2h5x

Publication Abstract from PubMed

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.

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 Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):731-4. Epub 2006 Jul 24. PMID:16880543^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.