2ZTE

MtRuvA Form IV

2ZTE の概要

• エントリーDOI: 10.2210/pdb2zte/pdb
• 関連するPDBエントリー: 2H5X 2ZTC 2ZTD
• 分子名称: Holliday junction ATP-dependent DNA helicase ruvA (2 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21870.08

構造登録者

Prabu, J.R.,Thamotharan, S.,Khanduja, J.S.,Chandra, N.R.,Muniyappa, K.,Vijayan, M. (登録日: 2008-10-01, 公開日: 2009-05-05, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.2 Å)