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Literature summary for 3.4.25.1 extracted from
- Structure characterization of the 26S proteasome (2011), Biochim. Biophys. Acta, 1809, 67-79.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified 20S protease core, X-ray diffraction structure determination and analysis | Escherichia coli |
| purified 20S protease core, X-ray diffraction structure determination and analysis | Homo sapiens |
| purified 20S protease core, X-ray diffraction structure determination and analysis | Saccharomyces cerevisiae |
| purified 20S protease core, X-ray diffraction structure determination and analysis | Thermoplasma acidophilum |
| purified 20S protease core, X-ray diffraction structure determination and analysis | Mycobacterium tuberculosis |
| purified 20S protease core, X-ray diffraction structure determination and analysis | Methanocaldococcus jannaschii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Methanocaldococcus jannaschii | - |
- |
- |
| Mycobacterium tuberculosis | - |
- |
- |
| Saccharomyces cerevisiae | - |
- |
- |
| Thermoplasma acidophilum | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings | Escherichia coli |
| More | three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings | Mycobacterium tuberculosis |
| More | three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The archaeal alpha and beta rings are each composed of seven identical subunits, thus the archaeal 20S CP has true D7-symmetry | Thermoplasma acidophilum |
| More | three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The archaeal alpha and beta rings are each composed of seven identical subunits, thus the archaeal 20S CP has true D7-symmetry | Methanocaldococcus jannaschii |
| More | three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The eukaryotic alpha and beta rings are each composed of seven distinct homologous subunits, which form a pseudo 7fold symmetrical structure of alpha1-7beta1-7beta1-7alpha1-7, with proteolytic active sites located at the N-termini of three subunits, beta1, beta2 and beta5, of each beta-ring. Another form of proteasome, called immunoproteasome, in which three beta-subunits of the normal 20S, beta1, beta2, beta5 are replaced by three IFN-gamma induced beta-subunits, beta1i, beta2i, beta5i. ATPase induced gate opening in the 20S CP | Homo sapiens |
| More | three-dimensional structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, detailed overview. Simple assembly process of the 20S proteasome. The 20S proteasome shows a hollow barrel-shaped structure with C2 symmetry composed of four stacked rings: two inner beta rings and two outer alpha rings. The eukaryotic alpha and beta rings are each composed of seven distinct homologous subunits, which form a pseudo 7fold symmetrical structure of alpha17beta17beta17alpha17, with proteolytic active sites located at the N-termini of three subunits, beta1, beta2 and beta5, of each beta-ring | Saccharomyces cerevisiae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 20S CP | - |
Escherichia coli |
| 20S CP | - |
Homo sapiens |
| 20S CP | - |
Saccharomyces cerevisiae |
| 20S CP | - |
Thermoplasma acidophilum |
| 20S CP | - |
Mycobacterium tuberculosis |
| 20S CP | - |
Methanocaldococcus jannaschii |
| 20S protease core | - |
Escherichia coli |
| 20S protease core | - |
Homo sapiens |
| 20S protease core | - |
Saccharomyces cerevisiae |
| 20S protease core | - |
Thermoplasma acidophilum |
| 20S protease core | - |
Mycobacterium tuberculosis |
| 20S protease core | - |
Methanocaldococcus jannaschii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | dependent on | Escherichia coli |  |
| ATP | dependent on | Homo sapiens | |
| ATP | dependent on | Saccharomyces cerevisiae | |
| ATP | dependent on | Thermoplasma acidophilum | |
| ATP | dependent on | Mycobacterium tuberculosis | |
| ATP | dependent on | Methanocaldococcus jannaschii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview | Escherichia coli |
| additional information | structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview | Homo sapiens |
| additional information | structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview | Saccharomyces cerevisiae |
| additional information | structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview | Thermoplasma acidophilum |
| additional information | structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview | Mycobacterium tuberculosis |
| additional information | structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview | Methanocaldococcus jannaschii |
| physiological function | the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable | Escherichia coli |
| physiological function | the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable | Saccharomyces cerevisiae |
| physiological function | the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable | Thermoplasma acidophilum |
| physiological function | the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable | Mycobacterium tuberculosis |
| physiological function | the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable | Methanocaldococcus jannaschii |
| physiological function | the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable. Immunoproteasome is responsible for breaking down foreign proteins into short antigenic peptides, which are ligands of MHC class I molecules. ATPase induced gate opening in the 20S CP | Homo sapiens |
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