2ZTD

MtRuvA Form III

Summary for 2ZTD

• Entry DOI: 10.2210/pdb2ztd/pdb
• Related: 2H5X 2ZTC 2ZTE
• Descriptor: Holliday junction ATP-dependent DNA helicase ruvA, GLYCEROL (3 entities in total)
• Functional Keywords: recombination, branch migration, holliday junction, dna binding, oligomerization, acidic pin, dna binding protein, atp-binding, dna damage, dna recombination, dna repair, dna-binding, helicase, hydrolase, nucleotide-binding, sos response
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 44108.53

Authors

Prabu, J.R.,Thamotharan, S.,Khanduja, J.S.,Chandra, N.R.,Muniyappa, K.,Vijayan, M. (deposition date: 2008-10-01, release date: 2009-05-05, Last modification date: 2023-11-01)

Primary citation

Prabu, J.R.,Thamotharan, S.,Khanduja, J.S.,Chandra, N.R.,Muniyappa, K.,Vijayan, M.
Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA Additional role of RuvB-binding domain and inter species variability
Biochim.Biophys.Acta, 1794:1001-1009, 2009

PubMed 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.

PubMed: 19374958
DOI: 10.1016/j.bbapap.2009.04.003

Experimental method

X-RAY DIFFRACTION (2.4 Å)