1bvq
From Proteopedia
(New page: 200px<br /><applet load="1bvq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bvq, resolution 2.0Å" /> '''THREE-DIMENSIONAL STR...) |
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| - | [[Image:1bvq.gif|left|200px]]<br /><applet load="1bvq" size=" | + | [[Image:1bvq.gif|left|200px]]<br /><applet load="1bvq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bvq, resolution 2.0Å" /> | caption="1bvq, resolution 2.0Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF 4-HYDROXYBENZOYL COA THIOESTERASE FROM PSEUDOMONAS SP. STRAIN CBS-3.'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF 4-HYDROXYBENZOYL COA THIOESTERASE FROM PSEUDOMONAS SP. STRAIN CBS-3.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The soil-dwelling microbe, Pseudomonas sp. strain CBS-3, has attracted | + | 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== | ==About this Structure== | ||
| - | 1BVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with EPE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1BVQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas sp.]] | [[Category: Pseudomonas sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Benning, M | + | [[Category: Benning, M M.]] |
[[Category: Dunaway-Mariano, D.]] | [[Category: Dunaway-Mariano, D.]] | ||
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
[[Category: EPE]] | [[Category: EPE]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:34 2008'' |
Revision as of 09:59, 21 February 2008
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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 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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