1Q4S

Crystal structure of Arthrobacter sp. strain SU 4-hydroxybenzoyl CoA thioesterase complexed with CoA and 4-hydroxybenzoic acid

1Q4S の概要

• エントリーDOI: 10.2210/pdb1q4s/pdb
• 関連するPDBエントリー: 1Q4T 1Q4U
• 分子名称: Thioesterase, COENZYME A, P-HYDROXYBENZOIC ACID, ... (4 entities in total)
• 機能のキーワード: thioesterase, hot-dog, hydrolase
• 由来する生物種: Arthrobacter sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34644.17

構造登録者

Thoden, J.B.,Zhuang, Z.,Dunaway-Mariano, D.,Holden, H.M. (登録日: 2003-08-04, 公開日: 2003-09-23, 最終更新日: 2024-02-14)

主引用文献

Thoden, J.B.,Zhuang, Z.,Dunaway-Mariano, D.,Holden, H.M.
The Structure of 4-Hydroxybenzoyl-CoA Thioesterase from Arthrobacter sp. strain SU
J.Biol.Chem., 278:43709-43716, 2003

PubMed Abstract: The 4-chlorobenzoyl-CoA dehalogenation pathway in certain Arthrobacter and Pseudomonas bacterial species contains three enzymes: a ligase, a dehalogenase, and a thioesterase. Here we describe the high resolution x-ray crystallographic structure of the 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU. The tetrameric enzyme is a dimer of dimers with each subunit adopting the so-called "hot dog fold" composed of six strands of anti-parallel beta-sheet flanked on one side by a rather long alpha-helix. The dimers come together to form the tetramer with their alpha-helices facing outwards. This quaternary structure is in sharp contrast to that previously observed for the 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas species strain CBS-3, whereby the dimers forming the tetramer pack with their alpha-helices projecting toward the interfacial region. In the Arthrobacter thioesterase, each of the four active sites is formed by three of the subunits of the tetramer. On the basis of both structural and kinetic data, it appears that Glu73 is the active site base in the Arthrobacter thioesterase. Remarkably, this residue is located on the opposite side of the substrate-binding pocket compared with that observed for the Pseudomonas enzyme. Although these two bacterial thioesterases demonstrate equivalent catalytic efficiencies, substrate specificities, and metabolic functions, their quaternary structures, CoA-binding sites, and catalytic platforms are decidedly different.

PubMed: 12907670
DOI: 10.1074/jbc.M308198200

実験手法

X-RAY DIFFRACTION (1.95 Å)