1BVQ
THREE-DIMENSIONAL STRUCTURE OF 4-HYDROXYBENZOYL COA THIOESTERASE FROM PSEUDOMONAS SP. STRAIN CBS-3.
Summary for 1BVQ
| Entry DOI | 10.2210/pdb1bvq/pdb |
| Descriptor | PROTEIN (4-HYDROXYBENZOYL COA THIOESTERASE), 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (3 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Pseudomonas sp. CBS3 |
| Total number of polymer chains | 1 |
| Total formula weight | 16378.76 |
| Authors | Holden, H.M.,Benning, M.M.,Dunaway-Mariano, D. (deposition date: 1998-09-16, release date: 1998-09-23, Last modification date: 2024-02-07) |
| Primary citation | 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 Cited by 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: 9837940DOI: 10.1074/jbc.273.50.33572 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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