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1QZM

alpha-domain of ATPase

1QZM の概要
エントリーDOI10.2210/pdb1qzm/pdb
分子名称ATP-dependent protease La (2 entities in total)
機能のキーワードoligomerization domain, aaa+ protein, atp-dependent protease, hydrolase
由来する生物種Escherichia coli
細胞内の位置Cytoplasm: P0A9M0
タンパク質・核酸の鎖数1
化学式量合計10838.53
構造登録者
Botos, I.,Melnikov, E.E.,Cherry, S.,Khalatova, A.G.,Rasulova, F.S.,Tropea, J.E.,Maurizi, M.R.,Rotanova, T.V.,Gustchina, A.,Wlodawer, A. (登録日: 2003-09-17, 公開日: 2004-05-04, 最終更新日: 2024-02-14)
主引用文献Botos, I.,Melnikov, E.E.,Cherry, S.,Khalatova, A.G.,Rasulova, F.S.,Tropea, J.E.,Maurizi, M.R.,Rotanova, T.V.,Gustchina, A.,Wlodawer, A.
Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.
J.Struct.Biol., 146:113-122,
Cited by
PubMed Abstract: The crystal structure of the small, mostly helical alpha domain of the AAA+ module of the Escherichia coli ATP-dependent protease Lon has been solved by single isomorphous replacement combined with anomalous scattering and refined at 1.9A resolution to a crystallographic R factor of 17.9%. This domain, comprising residues 491-584, was obtained by chymotrypsin digestion of the recombinant full-length protease. The alpha domain of Lon contains four alpha helices and two parallel strands and resembles similar domains found in a variety of ATPases and helicases, including the oligomeric proteases HslVU and ClpAP. The highly conserved "sensor-2" Arg residue is located at the beginning of the third helix. Detailed comparison with the structures of 11 similar domains established the putative location of the nucleotide-binding site in this first fragment of Lon for which a crystal structure has become available.
PubMed: 15037242
DOI: 10.1016/j.jsb.2003.09.003
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 1qzm
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2026-04-29に公開中

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