2h5x

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Revision as of 09:26, 21 November 2007

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spinqualitylabelsall models 2h5x, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

RuvA from Mycobacterium tuberculosis

Overview

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.

About this Structure

2H5X is a Single protein structure of sequence from Mycobacterium tuberculosis with GOL as ligand. Full crystallographic information is available from OCA.

Reference

Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination., Prabu JR, Thamotharan S, Khanduja JS, Alipio EZ, Kim CY, Waldo GS, Terwilliger TC, Segelke B, Lekin T, Toppani D, Hung LW, Yu M, Bursey E, Muniyappa K, Chandra NR, Vijayan M, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):731-4. Epub 2006 Jul 24. PMID:16880543

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