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Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.

J Rajan JR Prabu, S S Thamotharan, Jasbeer Singh JS Khanduja, Emily Zabala EZ Alipio, Chang Yub CY Kim, Geoffrey S GS Waldo, Thomas C TC Terwilliger, Brent B Segelke, Tim T Lekin, Dominique D Toppani, Li Wei LW Hung, Minmin M Yu, Evan E Bursey, K K Muniyappa, Nagasuma R NR Chandra, and M M Vijayan

Acta Crystallogr Sect F Struct Biol Cry... 62(Pt 8):731-4 (2006) PMID 16880543 PMCID 2242936

The process of recombinational repair is crucial for maintaining genomic integrity and generating biological diversity. In association with RuvB and RuvC, RuvA plays a central role in processing and resolving Holliday junctions, which are a critical intermediate in homologous recombination. Here, the cloning, purification and structure determination of the RuvA protein from Mycobacterium tuberculosis (MtRuvA) are reported. Analysis of the structure and comparison with other known RuvA proteins reveal an octameric state with conserved subunit-subunit interaction surfaces, indicating the requirement of octamer formation for biological activity. A detailed analysis of plasticity in the RuvA molecules has led to insights into the invariant and variable regions, thus providing a framework for understanding regional flexibility in various aspects of RuvA function.

DOI: 10.1107/S1744309106024791
Version: za2963e q8za3 q8zbc q8zc5 q8zd3 q8ze5 q8zfd q8zga
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