Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt 8):731-4. doi: 10.1107/S1744309106024791. Epub 2006 Jul 24.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics*
  • Binding Sites
  • Crystallography, X-Ray
  • DNA Helicases / chemistry*
  • DNA Helicases / genetics*
  • Models, Molecular
  • Mycobacterium tuberculosis / genetics*
  • Protein Conformation
  • Recombination, Genetic*


  • Bacterial Proteins
  • DNA Helicases

Associated data

  • PDB/2H5X