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

Prabu, J Rajan and Thamotharan, S and Khanduja, Jasbeer Singh and Chandra, Nagasuma R and Muniyappa, K and Vijayan, M (2009) Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA: Additional role of RuvB-binding domain and inter species variability. In: Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics, 1794 (7). pp. 1001-1009.

PDF fulltext.pdf - Published Version Restricted to Registered users only Download (828kB) | Request a copy

Abstract

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.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Keywords:	Recombination;Branch migration;Holliday junction;DNA binding; Oligomerization;Acidic pin.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit Division of Biological Sciences > Biochemistry
Date Deposited:	15 Jul 2009 04:40
Last Modified:	19 Sep 2010 05:36
URI:	http://eprints.iisc.ac.in/id/eprint/21142

Actions (login required)

View Item