Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA

Ariza, Antonio, Richard, Derek J., White, Malcolm F., & Bond, Charles S. (2005) Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA. Nucleic Acids Research, 33(5), p. 1465.

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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. 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 RadA molecule in the filament is linked to its neighbour via interactions of a short b-strand with the neighbouring ATPase domain. However, despite apparent flexibility between domains, comparison with other structures indicates conservation of a number of key interactions that introduce rigidity to the system, allowing allosteric control of the filament by interaction with ATP. Additional analysis reveals that the interaction specificity of the five human Rad51 paralogues can be predicted using a simple model based on the RadA structure.

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ID Code: 40651
Item Type: Journal Article
Refereed: Yes
Additional Information: Articles free to read on journal website
Keywords: Homologous recombinational repair, RadA, RecA, Rad51, Sulfolobus solfataricus
DOI: 10.1093/nar/gki288
ISSN: 1362-4962
Subjects: Australian and New Zealand Standard Research Classification > BIOLOGICAL SCIENCES (060000) > BIOCHEMISTRY AND CELL BIOLOGY (060100)
Divisions: Past > Schools > Cell & Molecular Biosciences
Past > QUT Faculties & Divisions > Faculty of Science and Technology
Copyright Owner: Copyright 2005 The Authors. Published by Oxford University Press. All rights reserved
Copyright Statement: The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact
Deposited On: 10 Mar 2011 03:32
Last Modified: 29 Jan 2015 01:33

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