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1bvq

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|PDB= 1bvq |SIZE=350|CAPTION= <scene name='initialview01'>1bvq</scene>, resolution 2.0&Aring;
|PDB= 1bvq |SIZE=350|CAPTION= <scene name='initialview01'>1bvq</scene>, resolution 2.0&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene>
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|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/4-chlorobenzoate_dehalogenase 4-chlorobenzoate dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.6 3.8.1.6]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/4-chlorobenzoate_dehalogenase 4-chlorobenzoate dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.6 3.8.1.6] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvq OCA], [http://www.ebi.ac.uk/pdbsum/1bvq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bvq RCSB]</span>
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[[Category: Dunaway-Mariano, D.]]
[[Category: Dunaway-Mariano, D.]]
[[Category: Holden, H M.]]
[[Category: Holden, H M.]]
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[[Category: EPE]]
 
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:16:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:09:14 2008''

Revision as of 16:09, 30 March 2008


PDB ID 1bvq

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands:
Activity: 4-chlorobenzoate dehalogenase, with EC number 3.8.1.6
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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.. 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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