5XTU
Crystal Structure of GDSL Esterase of Photobacterium sp. J15
5XTU の概要
| エントリーDOI | 10.2210/pdb5xtu/pdb |
| 分子名称 | GDSL-family esterase, DI(HYDROXYETHYL)ETHER, CHLORIDE ION, ... (8 entities in total) |
| 機能のキーワード | gdsl, sgnh, esterase, hydrolase, photobacterium |
| 由来する生物種 | Photobacterium sp. J15(2011) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 39809.33 |
| 構造登録者 | Mazlan, S.N.H.S.,Jonet, M.A.,Leow, T.C.,Ali, M.S.M.,Rahman, R.N.Z.R.A. (登録日: 2017-06-21, 公開日: 2018-10-10, 最終更新日: 2025-04-09) |
| 主引用文献 | Mazlan, S.N.H.S.,Ali, M.S.M.,Rahman, R.N.Z.R.A.,Sabri, S.,Jonet, M.A.,Leow, T.C. Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15. Int. J. Biol. Macromol., 119:1188-1194, 2018 Cited by PubMed Abstract: GDSL esterase J15 (EstJ15) is a member of Family II of lipolytic enzyme. The enzyme was further classified in subgroup SGNH hydrolase due to the presence of highly conserve motif, Ser-Gly-Asn-His in four conserved blocks I, II, III, and V, respectively. X-ray quality crystal of EstJ15 was obtained from optimized formulation containing 0.10 M ammonium sulphate, 0.15 M sodium cacodylate trihydrate pH 6.5, and 20% PEG 8000. The crystal structure of EstJ15 was solved at 1.38 Å with one molecule per asymmetric unit. The structure exhibits α/β hydrolase fold and shared low amino acid sequence identity of 23% with the passenger domain of the autotransporter EstA of Pseudomonas aeruginosa. The active site is located at the centre of the structure, formed a narrow tunnel that hinder long substrates to be catalysed which was proven by the protein-ligand docking analysis. This study facilitates the understanding of high substrate specificity of EstJ15 and provide insights on its catalytic mechanism. PubMed: 30102982DOI: 10.1016/j.ijbiomac.2018.08.022 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.38 Å) |
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