Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination

Kim, Chang-Yub ; Rajan Prabu, J. ; Alipio, Emily Zabala ; Waldo, Geoffrey S. ; Thamotharan, S. ; Khanduja, Jasbeer Singh ; Lekin, Tim ; Hung, Li-Wei ; Yu, Minmin ; Terwilliger, Thomas C. ; Segelke, Brent ; Toppani, Dominique ; Bursey, Evan ; Muniyappa, K. ; Chandra, Nagasuma R. ; Vijayan, M. (2006) Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination Acta Crystallographica Section F, 62 (8). pp. 731-734. ISSN 1744-3091

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Official URL: http://www3.interscience.wiley.com/journal/1185576...

Related URL: http://dx.doi.org/10.1107/S1744309106024791

Abstract

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.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:RuvA; Mycobacterium Tuberculosis; Recombinational Repair
ID Code:22476
Deposited On:24 Nov 2010 08:32
Last Modified:17 May 2016 06:30

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