1QZM
alpha-domain of ATPase
1QZM の概要
| エントリーDOI | 10.2210/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: 15037242DOI: 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) |
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