This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2bke
From Proteopedia
|
CONFORMATIONAL FLEXIBILITY REVEALED BY THE CRYSTAL STRUCTURE OF A CRENARCHAEAL RADA
Overview
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 single- and double-stranded DNA. The, recombinase molecules present in the archaea (RadA) and eukaryota (Rad51), are more closely related to each other than to their bacterial counterpart, (RecA) and, as a result, RadA makes a suitable model for the eukaryotic, system. The crystal structure of Sulfolobus solfataricus RadA has been, solved to a resolution of 3.2 A in the absence of nucleotide analogues or, DNA, revealing a narrow filamentous assembly with three molecules per, helical turn. As observed in other RecA-family recombinases, each ... [(full description)]
About this Structure
2BKE is a [Single protein] structure of sequence from [Sulfolobus solfataricus] with CL as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA., Ariza A, Richard DJ, White MF, Bond CS, Nucleic Acids Res. 2005 Mar 8;33(5):1465-73. Print 2005. PMID:15755748
Page seeded by OCA on Tue Oct 30 16:40:31 2007
Categories: Single protein | Sulfolobus solfataricus | Ariza, A. | Bond, C.S. | Richard, D.L. | White, M.F. | CL | Archaea | Dna repair | Dna-binding protei | Filament | Homologous recombination | Rad51 | Rada | Reca
