1q4s
From Proteopedia
(New page: 200px<br /><applet load="1q4s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q4s, resolution 1.95Å" /> '''Crystal structure of...) |
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| - | [[Image:1q4s.jpg|left|200px]]<br /><applet load="1q4s" size=" | + | [[Image:1q4s.jpg|left|200px]]<br /><applet load="1q4s" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1q4s, resolution 1.95Å" /> | caption="1q4s, resolution 1.95Å" /> | ||
'''Crystal structure of Arthrobacter sp. strain SU 4-hydroxybenzoyl CoA thioesterase complexed with CoA and 4-hydroxybenzoic acid'''<br /> | '''Crystal structure of Arthrobacter sp. strain SU 4-hydroxybenzoyl CoA thioesterase complexed with CoA and 4-hydroxybenzoic acid'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 4-chlorobenzoyl-CoA dehalogenation pathway in certain Arthrobacter and | + | The 4-chlorobenzoyl-CoA dehalogenation pathway in certain Arthrobacter and Pseudomonas bacterial species contains three enzymes: a ligase, a dehalogenase, and a thioesterase. Here we describe the high resolution x-ray crystallographic structure of the 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU. The tetrameric enzyme is a dimer of dimers with each subunit adopting the so-called "hot dog fold" composed of six strands of anti-parallel beta-sheet flanked on one side by a rather long alpha-helix. The dimers come together to form the tetramer with their alpha-helices facing outwards. This quaternary structure is in sharp contrast to that previously observed for the 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas species strain CBS-3, whereby the dimers forming the tetramer pack with their alpha-helices projecting toward the interfacial region. In the Arthrobacter thioesterase, each of the four active sites is formed by three of the subunits of the tetramer. On the basis of both structural and kinetic data, it appears that Glu73 is the active site base in the Arthrobacter thioesterase. Remarkably, this residue is located on the opposite side of the substrate-binding pocket compared with that observed for the Pseudomonas enzyme. Although these two bacterial thioesterases demonstrate equivalent catalytic efficiencies, substrate specificities, and metabolic functions, their quaternary structures, CoA-binding sites, and catalytic platforms are decidedly different. |
==About this Structure== | ==About this Structure== | ||
| - | 1Q4S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.] with COA and PHB as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA_thioesterase 4-hydroxybenzoyl-CoA thioesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.23 3.1.2.23] Full crystallographic information is available from [http:// | + | 1Q4S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_sp. Arthrobacter sp.] with <scene name='pdbligand=COA:'>COA</scene> and <scene name='pdbligand=PHB:'>PHB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxybenzoyl-CoA_thioesterase 4-hydroxybenzoyl-CoA thioesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.23 3.1.2.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dunaway-Mariano, D.]] | [[Category: Dunaway-Mariano, D.]] | ||
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
| - | [[Category: Thoden, J | + | [[Category: Thoden, J B.]] |
[[Category: Zhuang, Z.]] | [[Category: Zhuang, Z.]] | ||
[[Category: COA]] | [[Category: COA]] | ||
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[[Category: thioesterase]] | [[Category: thioesterase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:35:53 2008'' |
Revision as of 12:35, 21 February 2008
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Crystal structure of Arthrobacter sp. strain SU 4-hydroxybenzoyl CoA thioesterase complexed with CoA and 4-hydroxybenzoic acid
Overview
The 4-chlorobenzoyl-CoA dehalogenation pathway in certain Arthrobacter and Pseudomonas bacterial species contains three enzymes: a ligase, a dehalogenase, and a thioesterase. Here we describe the high resolution x-ray crystallographic structure of the 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU. The tetrameric enzyme is a dimer of dimers with each subunit adopting the so-called "hot dog fold" composed of six strands of anti-parallel beta-sheet flanked on one side by a rather long alpha-helix. The dimers come together to form the tetramer with their alpha-helices facing outwards. This quaternary structure is in sharp contrast to that previously observed for the 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas species strain CBS-3, whereby the dimers forming the tetramer pack with their alpha-helices projecting toward the interfacial region. In the Arthrobacter thioesterase, each of the four active sites is formed by three of the subunits of the tetramer. On the basis of both structural and kinetic data, it appears that Glu73 is the active site base in the Arthrobacter thioesterase. Remarkably, this residue is located on the opposite side of the substrate-binding pocket compared with that observed for the Pseudomonas enzyme. Although these two bacterial thioesterases demonstrate equivalent catalytic efficiencies, substrate specificities, and metabolic functions, their quaternary structures, CoA-binding sites, and catalytic platforms are decidedly different.
About this Structure
1Q4S is a Single protein structure of sequence from Arthrobacter sp. with and as ligands. Active as 4-hydroxybenzoyl-CoA thioesterase, with EC number 3.1.2.23 Full crystallographic information is available from OCA.
Reference
The structure of 4-hydroxybenzoyl-CoA thioesterase from arthrobacter sp. strain SU., Thoden JB, Zhuang Z, Dunaway-Mariano D, Holden HM, J Biol Chem. 2003 Oct 31;278(44):43709-16. Epub 2003 Aug 7. PMID:12907670
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