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2W0M

Crystal Structure of sso2452 from Sulfolobus solfataricus P2

2W0M の概要
エントリーDOI10.2210/pdb2w0m/pdb
分子名称SSO2452, ZINC ION, PYROPHOSPHATE 2-, ... (4 entities in total)
機能のキーワードsso2452, reca, sulfolobus solfataricus p2, sspf, unknown function
由来する生物種SULFOLOBUS SOLFATARICUS P2
タンパク質・核酸の鎖数1
化学式量合計27478.90
構造登録者
McRobbie, A.,Carter, L.,Johnson, K.A.,Kerou, M.,Liu, H.,Mcmahon, S.,Oke, M.,Naismith, J.H.,White, M.F. (登録日: 2008-08-19, 公開日: 2009-05-19, 最終更新日: 2023-12-13)
主引用文献Mcrobbie, A.M.,Carter, L.G.,Kerou, M.,Liu, H.,Mcmahon, S.A.,Johnson, K.A.,Oke, M.,Naismith, J.H.,White, M.F.
Structural and Functional Characterisation of a Conserved Archaeal Rada Paralog with Antirecombinase Activity.
J.Mol.Biol., 389:661-, 2009
Cited by
PubMed Abstract: DNA recombinases (RecA in bacteria, Rad51 in eukarya and RadA in archaea) catalyse strand exchange between homologous DNA molecules, the central reaction of homologous recombination, and are among the most conserved DNA repair proteins known. RecA is the sole protein responsible for this reaction in bacteria, whereas there are several Rad51 paralogs that cooperate to catalyse strand exchange in eukaryotes. All archaea have at least one (and as many as four) RadA paralog, but their function remains unclear. Herein, we show that the three RadA paralogs encoded by the Sulfolobus solfataricus genome are expressed under normal growth conditions and are not UV inducible. We demonstrate that one of these proteins, Sso2452, which is representative of the large archaeal RadC subfamily of archaeal RadA paralogs, functions as an ATPase that binds tightly to single-stranded DNA. However, Sso2452 is not an active recombinase in vitro and inhibits D-loop formation by RadA. We present the high-resolution crystal structure of Sso2452, which reveals key structural differences from the canonical RecA family recombinases that may explain its functional properties. The possible roles of the archaeal RadA paralogs in vivo are discussed.
PubMed: 19414020
DOI: 10.1016/J.JMB.2009.04.060
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 2w0m
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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