2bke | pdb_00002bke
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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
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