1EVQ

THE CRYSTAL STRUCTURE OF THE THERMOPHILIC CARBOXYLESTERASE EST2 FROM ALICYCLOBACILLUS ACIDOCALDARIUS

1EVQ の概要

• エントリーDOI: 10.2210/pdb1evq/pdb
• 分子名称: SERINE HYDROLASE, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase fold, hydrolase
• 由来する生物種: Alicyclobacillus acidocaldarius
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34887.00

構造登録者

De Simone, G.,Galdiero, S.,Manco, G.,Lang, D.,Rossi, M.,Pedone, C. (登録日: 2000-04-20, 公開日: 2000-11-22, 最終更新日: 2024-12-25)

主引用文献

De Simone, G.,Galdiero, S.,Manco, G.,Lang, D.,Rossi, M.,Pedone, C.
A snapshot of a transition state analogue of a novel thermophilic esterase belonging to the subfamily of mammalian hormone-sensitive lipase.
J.Mol.Biol., 303:761-771, 2000

PubMed Abstract: EST2 is a novel thermophilic carboxylesterase, isolated and cloned from Alicyclobacillus (formerly Bacillus) acidocaldarius, which optimally hydrolyses esters with acyl chain lengths of six to eight carbon atoms at 70 degrees C. On the basis of the amino acid sequence homology, it has been classified as a member of the mammalian hormone-sensitive lipase (HSL) subfamily. The crystal structure of EST2, complexed with a sulphonyl derivative, has been determined at 2.6 A resolution by a multiple wavelength anomalous diffraction experiment on a seleno-methionine derivative. EST2 presents a canonical alpha/beta hydrolase core, shielded at the C-terminal side by a cap region built up of five helices. It contains the lipase-like catalytic triad, Ser155, His282 and Asp252, whereby the nucleophile is covalently modified. This allows an unambiguous view of the putative active site of EST2, detecting the oxyanion hole, in whose formation the amino acid sequence motif His81-Gly82-Gly83-Gly84 is involved, and the hydrophobic binding pocket for the acyl chain. The structural model here reported provides the first example of a transition state analogue of an esterase/lipase belonging to the HSL group, thus affording useful information for the design of medical inhibitors. Moreover, as the first X-ray structure of a thermophilic carboxylesterase, the comparison with its mesophilic homologue, the Brefeldin A esterase (BFAE) from Bacillus subtilis, allows the identification of putative determinants of thermal stability.

PubMed: 11061974
DOI: 10.1006/jmbi.2000.4195

実験手法

X-RAY DIFFRACTION (2.6 Å)