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Literature summary for 3.6.4.B9 extracted from

  • Haseltine, C.A.; Kowalczykowski, S.C.
    An archaeal Rad54 protein remodels DNA and stimulates DNA strand exchange by RadA (2009), Nucleic Acids Res., 37, 2757-2770.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
double-strand DNA double-strand DNA-dependent ATPase. The protein itself has a low level of ATP hydrolysis activity, which is not increased by the addition of the ssDNA, poly(dA). Stimulation of ATPase activity is obtained using dsDNA [poly(dA)/poly(dT)] as the substrate Saccharolobus solfataricus
dsDNA double-strand DNA-dependent ATPase. The protein itself has a low level of ATP hydrolysis activity, which is not increased by the addition of the ssDNA, poly(dA). Stimulation of ATPase activity is obtained using dsDNA [poly(dA)/poly(dT)] as the substrate Saccharolobus solfataricus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method at 25°C, crystals of SsoRad54cd in complex with a 25-mer DNA duplex are refined to 3.0 A resolution. 2.0 A resolution structure of crystals of the C-terminal half of SsoRad54cd separately (residues 432–906) Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
E563Q DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is less than 5% of wild-type activity Saccharolobus solfataricus
G722Q DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 95% of wild-type activity Saccharolobus solfataricus
K700E DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 40% of wild-type activity Saccharolobus solfataricus
K711E DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 30% of wild-type activity Saccharolobus solfataricus
K808E DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 30% of wild-type activity Saccharolobus solfataricus
K872E DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 35% of wild-type activity Saccharolobus solfataricus
N569I mutation reduces both DNA-stimulated ATPase activity and DNA binding activity. DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 35% of wild-type activity Saccharolobus solfataricus
Q755A DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 40% of wild-type activity Saccharolobus solfataricus
R586W DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 80% of wild-type activity Saccharolobus solfataricus
R788E DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 10% of wild-type activity Saccharolobus solfataricus
R840E DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 5% of wild-type activity Saccharolobus solfataricus
R843E DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 5% of wild-type activity Saccharolobus solfataricus
V850G DNA (poly[dA:dT])-stimulated ATP hydrolysis activity is about 5% of wild-type activity Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
92853
-
x * 92853, calculated from sequence Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97XQ7
-
-
Saccharolobus solfataricus P2 Q97XQ7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O = ADP + phosphate the double-stranded DNA-dependent ATPase can alter the topology of the duplex DNA Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O a double-stranded DNA-dependent ATPase that can alter the topology of duplex DNA. It interacts directly with the Sulfolobus solfataricus Rad51 homologue, SsoRadA, to stimulate DNA strand exchange. No helicase activity Saccharolobus solfataricus ADP + phosphate
-
?
ATP + H2O the double-strand DNA-dependent ATPase that can alter the topology of duplex DNA. It interacts directly with the Sulfolobus solfataricus Rad51 homologue, SsoRadA, to stimulate DNA strand exchange. No helicase activity Saccharolobus solfataricus ADP + phosphate
-
?
ATP + H2O a double-stranded DNA-dependent ATPase that can alter the topology of duplex DNA. It interacts directly with the Sulfolobus solfataricus Rad51 homologue, SsoRadA, to stimulate DNA strand exchange. No helicase activity Saccharolobus solfataricus P2 ADP + phosphate
-
?
ATP + H2O the double-strand DNA-dependent ATPase that can alter the topology of duplex DNA. It interacts directly with the Sulfolobus solfataricus Rad51 homologue, SsoRadA, to stimulate DNA strand exchange. No helicase activity Saccharolobus solfataricus P2 ADP + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 92853, calculated from sequence Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
dsDNA translocase
-
Saccharolobus solfataricus
Rad54 protein
-
Saccharolobus solfataricus
SSO1653 locus name Saccharolobus solfataricus
SsoRad54
-
Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Saccharolobus solfataricus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
50 70 50°C: about 80% of maximal activity, 70°C: about 60% of maximal activity Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Saccharolobus solfataricus