Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA Additional role of RuvB-binding domain and inter species variability

Biochim Biophys Acta. 2009 Jul;1794(7):1001-9. doi: 10.1016/j.bbapap.2009.04.003. Epub 2009 Apr 15.


RuvA, along with RuvB, is involved in branch migration of heteroduplex DNA in homologous recombination. The structures of three new crystal forms of RuvA from Mycobacterium tuberculosis (MtRuvA) have been determined. The RuvB-binding domain is cleaved off in one of them. Detailed models of the complexes of octameric RuvA from different species with the Holliday junction have also been constructed. A thorough examination of the structures presented here and those reported earlier brings to light the hitherto unappreciated role of the RuvB-binding domain in determining inter-domain orientation and oligomerization. These structures also permit an exploration of the interspecies variability of structural features such as oligomerization and the conformation of the loop that carries the acidic pin, in terms of amino acid substitutions. These models emphasize the additional role of the RuvB-binding domain in Holliday junction binding. This role along with its role in oligomerization could have important biological implications.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • DNA Primers
  • Models, Molecular*
  • Molecular Sequence Data
  • Mycobacterium tuberculosis / chemistry*
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Species Specificity


  • Bacterial Proteins
  • DNA Primers