1bvq

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

spinqualitylabelsall models 1bvq, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bvq is a 1 chain structure with sequence from Pseuc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EPE Activity: 4-chlorobenzoate dehalogenase, with EC number 3.8.1.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [4HBT_PSEUC] Hydrolyzes 4-hydroxybenzoate-CoA, and to a lesser extent benzoyl-CoA and 4-chlorobenzoate-CoA. Not active against aliphatic acyl-CoA thioesters, including palmitoyl-CoA, hexanoyl-CoA and acetyl-CoA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioesterase

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