1bvq

<table><tr><td colspan='2'>[[1bvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._cbs3 Pseudomonas sp. cbs3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BVQ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-chlorobenzoate_dehalogenase 4-chlorobenzoate dehalogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.6 3.8.1.6] </span></td></tr>

[[https://www.uniprot.org/uniprot/4HBT_PSEUC 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.<ref>PMID:1610806</ref>

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== 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<ref>PMID:9837940</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1bvq" style="background-color:#fffaf0;"></div>

[[Category: 4-chlorobenzoate dehalogenase]]

[[Category: Pseudomonas sp. cbs3]]

[[Category: Benning, M M]]

[[Category: Dunaway-Mariano, D]]

[[Category: Holden, H M]]

[[Category: Hydrolase]]