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Nucleic Acids Research 2005 33(5):1465-1473; doi:10.1093/nar/gki288
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Published online 8 March 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
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 journals.permissions{at}oupjournals.org

Article

Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA

Antonio Ariza, Derek J. Richard1, Malcolm F. White1 and Charles S. Bond*

Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee Dow St, Dundee, DD1 5EH, UK 1Centre for Biomolecular Sciences, University of St Andrews North Haugh, St Andrews, KY16 9ST, UK

*To whom correspondence should be addressed: Tel: +44 1382 348325; Fax: +44 1382 345764; Email: C.S.Bond{at}dundee.ac.uk

Received January 17, 2005. Revised February 18, 2005. Accepted February 18, 2005.

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 Å 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 ß-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.

Present address: Derek J. Richard, Queensland Institute of Medical Research, PO Royal Brisbane Hospital, Queensland 4029, Australia


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