Open AccessStructure of Mycobacterium tuberculosis RuvA, a protein involved in recombination
Author(s) -
Kim ChangYub,
Prabu J. Rajan,
Alipio Emily Zabala,
Waldo Geoffrey S.,
Thamotharan S.,
Khanduja Jasbeer Singh,
Lekin Tim,
Hung LiWei,
Yu Minmin,
Terwilliger Thomas C.,
Segelke Brent,
Toppani Dominique,
Bursey Evan,
Muniyappa K.,
Chandra Nagasuma R.,
Vijayan M.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106024791
Subject(s) - holliday junction , homologous recombination , biology , branch migration , genetics , histone octamer , microbiology and biotechnology , mycobacterium smegmatis , recombination , mycobacterium tuberculosis , computational biology , dna , gene , nucleosome , tuberculosis , medicine , pathology , histone
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.