1BVQ

THREE-DIMENSIONAL STRUCTURE OF 4-HYDROXYBENZOYL COA THIOESTERASE FROM PSEUDOMONAS SP. STRAIN CBS-3.

1BVQ の概要

• エントリーDOI: 10.2210/pdb1bvq/pdb
• 分子名称: PROTEIN (4-HYDROXYBENZOYL COA THIOESTERASE), 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Pseudomonas sp. CBS3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16378.76

構造登録者

Holden, H.M.,Benning, M.M.,Dunaway-Mariano, D. (登録日: 1998-09-16, 公開日: 1998-09-23, 最終更新日: 2024-02-07)

主引用文献

Benning, M.M.,Wesenberg, G.,Liu, R.,Taylor, K.L.,Dunaway-Mariano, D.,Holden, H.M.
The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3.
J.Biol.Chem., 273:33572-33579, 1998

PubMed Abstract: The soil-dwelling microbe, Pseudomonas sp. strain CBS-3, has attracted recent attention due to its ability to survive on 4-chlorobenzoate as its sole carbon source. The biochemical pathway by which this organism converts 4-chlorobenzoate to 4-hydroxybenzoate consists of three enzymes: 4-chlorobenzoyl-CoA ligase, 4-chlorobenzoyl-CoA dehalogenase, and 4-hydroxybenzoyl-CoA thioesterase. Here we describe the three-dimensional structure of the thioesterase determined to 2.0-A resolution. Each subunit of the homotetramer is characterized by a five-stranded anti-parallel beta-sheet and three major alpha-helices. While previous amino acid sequence analyses failed to reveal any similarity between this thioesterase and other known proteins, the results from this study clearly demonstrate that the molecular architecture of 4-hydroxybenzoyl-CoA thioesterase is topologically equivalent to that observed for beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli. On the basis of the structural similarity between these two enzymes, the active site of the thioesterase has been identified and a catalytic mechanism proposed.

PubMed: 9837940
DOI: 10.1074/jbc.273.50.33572

実験手法

X-RAY DIFFRACTION (2 Å)