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Literature summary for 3.6.4.B7 extracted from
- Nanobiomotors of archaeal DNA repair machineries: current research status and application potential (2014), Cell Biosci., 4, 32.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | RadC1 and RadC2 are involved in DNA repair | Sulfolobus islandicus | |
| additional information | RadC1 and RadC2 are involved in DNA repair | Thermoplasma acidophilum | |
| RadC1 | Sto0579, enhances the ATPase and strand invasion activities of RadA | Sulfurisphaera tokodaii | |
| RadC2 | Sto1830, interacts with both RadA and Hjc, a Holliday junction resolvase | Sulfurisphaera tokodaii |
Application
| Application | Comment | Organism |
|---|---|---|
| pharmacology | application potential of archaeal nanobiomotors in drug delivery | Archaeoglobus fulgidus |
| pharmacology | application potential of archaeal nanobiomotors in drug delivery | Sulfurisphaera tokodaii |
| pharmacology | application potential of archaeal nanobiomotors in drug delivery | Sulfolobus islandicus |
| pharmacology | application potential of archaeal nanobiomotors in drug delivery | Methanococcus voltae |
| pharmacology | application potential of archaeal nanobiomotors in drug delivery | Pyrococcus furiosus |
| pharmacology | application potential of archaeal nanobiomotors in drug delivery | Saccharolobus solfataricus |
| pharmacology | application potential of archaeal nanobiomotors in drug delivery | Thermoplasma acidophilum |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis, enzyme with bound AMP-PNP, PDB ID 1T4G | Methanococcus voltae |
| crystal structure analysis, PDB ID 1PZN | Pyrococcus furiosus |
| crystal structure analysis, PDB ID 1T4G | Archaeoglobus fulgidus |
| crystal structure analysis, PDB ID 1T4G | Sulfurisphaera tokodaii |
| crystal structure analysis, PDB ID 1T4G | Sulfolobus islandicus |
| crystal structure analysis, PDB ID 1T4G | Thermoplasma acidophilum |
| crystal structure analysis, PDB IDs 2DFL and 2BKE | Saccharolobus solfataricus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Archaeoglobus fulgidus |  |
| Mg2+ | required | Sulfurisphaera tokodaii | |
| Mg2+ | required | Sulfolobus islandicus | |
| Mg2+ | required | Methanococcus voltae | |
| Mg2+ | required | Pyrococcus furiosus | |
| Mg2+ | required | Saccharolobus solfataricus | |
| Mg2+ | required | Thermoplasma acidophilum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Archaeoglobus fulgidus | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Sulfurisphaera tokodaii | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Sulfolobus islandicus | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Methanococcus voltae | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Pyrococcus furiosus | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Saccharolobus solfataricus | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Thermoplasma acidophilum | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Saccharolobus solfataricus P2 | - |
ADP + phosphate | - |
? | |
| ATP + H2O | Thermoplasma acidophilum ATCC 25905 | - |
ADP + phosphate | - |
? | |
| additional information | Archaeoglobus fulgidus | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
| additional information | Sulfurisphaera tokodaii | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
| additional information | Sulfolobus islandicus | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
| additional information | Methanococcus voltae | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
| additional information | Pyrococcus furiosus | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
| additional information | Saccharolobus solfataricus | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
| additional information | Thermoplasma acidophilum | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
| additional information | Saccharolobus solfataricus P2 | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
| additional information | Thermoplasma acidophilum ATCC 25905 | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Archaeoglobus fulgidus | - |
- |
- |
| Methanococcus voltae | O73948 | - |
- |
| Pyrococcus furiosus | O74036 | - |
- |
| Saccharolobus solfataricus | Q55075 | - |
- |
| Saccharolobus solfataricus P2 | Q55075 | - |
- |
| Sulfolobus islandicus | - |
- |
- |
| Sulfurisphaera tokodaii | - |
- |
- |
| Thermoplasma acidophilum | Q9HJ68 | - |
- |
| Thermoplasma acidophilum ATCC 25905 | Q9HJ68 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Archaeoglobus fulgidus | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Sulfurisphaera tokodaii | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Sulfolobus islandicus | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Methanococcus voltae | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Pyrococcus furiosus | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Saccharolobus solfataricus | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Thermoplasma acidophilum | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Saccharolobus solfataricus P2 | ADP + phosphate | - |
? | |
| ATP + H2O | - |
Thermoplasma acidophilum ATCC 25905 | ADP + phosphate | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Archaeoglobus fulgidus | ? | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Sulfurisphaera tokodaii | ? | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Sulfolobus islandicus | ? | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Methanococcus voltae | ? | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Pyrococcus furiosus | ? | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Saccharolobus solfataricus | ? | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Thermoplasma acidophilum | ? | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Saccharolobus solfataricus P2 | ? | - |
? | |
| additional information | The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Formation of RadA-ssDNA filaments and stabilization, rotation mechanism of the enzyme nanobiomotor, overview | Thermoplasma acidophilum ATCC 25905 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme domain organization, overview | Archaeoglobus fulgidus |
| More | enzyme domain organization, overview | Sulfurisphaera tokodaii |
| More | enzyme domain organization, overview | Sulfolobus islandicus |
| More | enzyme domain organization, overview | Thermoplasma acidophilum |
| More | enzyme domain organization, structure comparisons, overview | Methanococcus voltae |
| More | enzyme domain organization, structure comparisons, overview | Pyrococcus furiosus |
| More | enzyme domain organization, structure comparisons, overview | Saccharolobus solfataricus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Rad51 | - |
Pyrococcus furiosus |
| Rad51 | - |
Thermoplasma acidophilum |
| RadA | - |
Archaeoglobus fulgidus |
| RadA | - |
Sulfurisphaera tokodaii |
| RadA | - |
Sulfolobus islandicus |
| RadA | - |
Methanococcus voltae |
| RadA | - |
Pyrococcus furiosus |
| RadA | - |
Saccharolobus solfataricus |
| RadA | - |
Thermoplasma acidophilum |
| RadC1 | - |
Archaeoglobus fulgidus |
| RadC2 | - |
Archaeoglobus fulgidus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea | Archaeoglobus fulgidus |
| evolution | the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea | Sulfurisphaera tokodaii |
| evolution | the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea | Sulfolobus islandicus |
| evolution | the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea | Saccharolobus solfataricus |
| evolution | the enzyme belongs to the RecA/RadA family of recombinase proteins of the AAA + ATPases, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea | Thermoplasma acidophilum |
| evolution | the enzyme belongs to the RecA/RadA family of recombinase proteins, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea | Methanococcus voltae |
| evolution | the enzyme belongs to the RecA/RadA family of recombinase proteins, including RecA proteins of bacteria, RadAs in archaea, Rad51 and DMC1 proteins in Eukaryotes. Archaea and eukaryotes encode RadA/Rad51 paralogues, such as Rad55/57 in yeast, Rad51B/C/D, Xrcc2 and Xrcc3 in mammals, and RadB, RadC in Archaea, which facilitate homologous recombination by interacting with RadA/Rad51 recombinases. Archaeal RadA and eukaryotic Rad51 proteins show high amino acid sequence identities to each other (over 40%) but they are more distantly related to bacterial RecA proteins, exhibiting about 20% sequence identity. Archaeal and eukaryotic recombinases are also more closely related to each other at protein domain structure. RadA paralogues represent another major group of AAA + ATPases involved in DNA damage repair in Archaea | Pyrococcus furiosus |
| metabolism | nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion | Archaeoglobus fulgidus |
| metabolism | nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion | Sulfurisphaera tokodaii |
| metabolism | nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion | Sulfolobus islandicus |
| metabolism | nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion | Methanococcus voltae |
| metabolism | nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion | Pyrococcus furiosus |
| metabolism | nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion | Saccharolobus solfataricus |
| metabolism | nanobiomotors perform various important functions in the cell, and they also emerge as potential vehicle for drug delivery. The proteins employ conserved ATPase domains to convert chemical energy to mechanical work and motion. Some are active during DNA damage repair. All nanobiomotors contain an ATPase domain that adopts RecA fold structure, characteristic for RecA/RadA family proteins, structural analyses of archaeal nucleic acid biomotors and the molecular mechanisms of how ATP binding and hydrolysis promote the conformation change that drives mechanical motion | Thermoplasma acidophilum |
| additional information | the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain | Archaeoglobus fulgidus |
| additional information | the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain | Sulfurisphaera tokodaii |
| additional information | the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain | Sulfolobus islandicus |
| additional information | the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain | Methanococcus voltae |
| additional information | the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain | Pyrococcus furiosus |
| additional information | the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain | Saccharolobus solfataricus |
| additional information | the ring and right-handed filament structures of RadAs, domain structure and organization, overview. In the absence of ATP, the Walker motifs adopt a conformation to hold the ATP-binding site open and do not interact with the adjacent ATPase domain | Thermoplasma acidophilum |
| physiological function | homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor | Thermoplasma acidophilum |
| physiological function | homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase | Sulfurisphaera tokodaii |
| physiological function | homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase | Sulfolobus islandicus |
| physiological function | homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase | Methanococcus voltae |
| physiological function | homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase | Pyrococcus furiosus |
| physiological function | homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essential mediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase | Saccharolobus solfataricus |
| physiological function | homologous recombination protein RadA/Rad51 recombinase binds to 3'-pertruding ends of dsDNA mediating the strand invasion reaction in homologous recombination. The recombinases are essentialmediators of homologous recombination, an activity that is required for repairing dsDNA breaks and re-starting of stalled DNA replication forks. The RecA/RadA-facilitated strand exchange reaction occurs in two steps: (a) the recombinases bind to ssDNA, forming a nucleoprotein complex, and (b) the nucleoprotein complex invades a homologous dsDNA, such that the invading RadA-ssDNA base pairs with the complimentary strand of the dsDNA whereas the other stranded of the DNA becomes ssDNA, forming a so-called D-loop structure. The D-loop structure is a very important intermediate in DNA repair or DNA replication processes. Rotation mechanism of the enzyme nanobiomotor. RadA provides a prototype nanobiomotor for studying conversion of chemical energy to mechanical movement. In the clockwise rotation model, ATP binding and hydrolysis at the core domain result in repositioning of NTD and core domain and rotation between two adjacent subunits. Unlike most nanobiomotors that translocate along DNA, RadA polymers do not move along ssDNA or dsDNA but rotate around the axis like F1 ATPase | Archaeoglobus fulgidus |
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Release 2023.1 (January 2023)
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