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Literature summary for 3.6.4.B7 extracted from

  • Ariza, A.; Richard, D.J.; White, M.F.; Bond, C.S.
    Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA (2005), Nucleic Acids Res., 33, 1465-1473.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.4.B7

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of full-length enzyme, quality crystals are grown at 4°C using the hanging drop vapour diffusion method against a reservoir containing 0.5 ml 0.1 M Tris–HCl, pH 9.5 with 10% (v/v) tert-butanol, resolution of 3.2 A. crystal structure reveals a conformation of fine filaments in the absence of nucleotides Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35867
-
 x * 35867, calculated from sequence Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q55075
-
-
Saccharolobus solfataricus P2 Q55075
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O = ADP + phosphate involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules Saccharolobus solfataricus
a

Subunits

Subunits Comment Organism
? x * 35867, calculated from sequence Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
RadA
-
 Saccharolobus solfataricus
SSO0250 locus name Saccharolobus solfataricus
SsRada
-
 Saccharolobus solfataricus

General Information

General Information Comment Organism
physiological function homologous recombinational repair is an essential mechanism for repair of double-strand breaks in DNA. Recombinases of the RecA-fold family play a crucial role in this process, forming filaments that utilize ATP to mediate their interactions with singleand double-stranded DNA Saccharolobus solfataricus