1bvq
From Proteopedia
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THREE-DIMENSIONAL STRUCTURE OF 4-HYDROXYBENZOYL COA THIOESTERASE FROM PSEUDOMONAS SP. STRAIN CBS-3.
Overview
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.
About this Structure
1BVQ is a Single protein structure of sequence from Pseudomonas sp. with EPE as ligand. Active as 4-chlorobenzoate dehalogenase, with EC number 3.8.1.6 Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3., Benning MM, Wesenberg G, Liu R, Taylor KL, Dunaway-Mariano D, Holden HM, J Biol Chem. 1998 Dec 11;273(50):33572-9. PMID:9837940
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