1q4t: Difference between revisions

Revision as of 06:45, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1q4t.png

Template:STRUCTURE 1q4t

crystal structure of 4-hydroxybenzoyl CoA thioesterase from Arthrobacter sp. strain SU complexed with 4-hydroxyphenyl CoAcrystal structure of 4-hydroxybenzoyl CoA thioesterase from Arthrobacter sp. strain SU complexed with 4-hydroxyphenyl CoA

Template:ABSTRACT PUBMED 12907670

About this StructureAbout this Structure

1Q4T is a Single protein structure of sequence from Arthrobacter sp.. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 06:45:17 2008

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 {{STRUCTURE_1q4t|  PDB=1q4t  |  SCENE=  }}
-'''crystal structure of 4-hydroxybenzoyl CoA thioesterase from Arthrobacter sp. strain SU complexed with 4-hydroxyphenyl CoA'''
+===crystal structure of 4-hydroxybenzoyl CoA thioesterase from Arthrobacter sp. strain SU complexed with 4-hydroxyphenyl CoA===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12907670}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12907670 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12907670}}
 ==About this Structure==
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 [[Category: Hot-dog]]
 [[Category: Thioesterase]]
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