View source for 1lo8

==X-ray crystal structure of 4-hydroxybenzoyl CoA thioesterase complexed with 4-hydroxybenzyl CoA==
<StructureSection load='1lo8' size='340' side='right' caption='[[1lo8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lo8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseuc Pseuc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LO8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LO8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CA:4-HYDROXYBENZYL+COENZYME+A'>4CA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lo7|1lo7]], [[1lo9|1lo9]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">4HBT_PSESP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=72586 PSEUC])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lo8 OCA], [http://pdbe.org/1lo8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lo8 RCSB], [http://www.ebi.ac.uk/pdbsum/1lo8 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/4HBT_PSEUC 4HBT_PSEUC]] Hydrolyzes 4-hydroxybenzoate-CoA, and to a lesser extent benzoyl-CoA and 4-chlorobenzoate-CoA. Not active against aliphatic acyl-CoA thioesters, including palmitoyl-CoA, hexanoyl-CoA and acetyl-CoA.<ref>PMID:1610806</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lo/1lo8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The metabolic pathway by which 4-chlorobenzoate is degraded to 4-hydroxybenzoate in the soil-dwelling microbe Pseudomonas sp. strain CBS-3 consists of three enzymes including 4-hydroxybenzoyl-CoA thioesterase. The structure of the unbound form of this thioesterase has been shown to contain the so-called "hot dog" fold with a large helix packed against a five-stranded anti-parallel beta-sheet. To address the manner in which the enzyme accommodates the substrate within the active site, two inhibitors have been synthesized, namely 4-hydroxyphenacyl-CoA and 4-hydroxybenzyl-CoA. Here we describe the structural analyses of the enzyme complexed with these two inhibitors determined and refined to 1.5 and 1.8 A resolution, respectively. These studies indicate that only one protein side chain, Ser(91), participates directly in ligand binding. All of the other interactions between the protein and the inhibitors are mediated through backbone peptidic NH groups, carbonyl oxygens, and/or solvents. The structures of the enzyme-inhibitor complexes suggest that both a hydrogen bond and the positive end of a helix dipole moment serve to polarize the electrons away from the carbonyl carbon of the acyl group, thereby making it more susceptible to nucleophilic attack. Additionally, these studies demonstrate that the carboxylate group of Asp(17) is approximately 3.2 A from the carbonyl carbon of the acyl group. To address the role of Asp(17), the structure of the site-directed mutant protein D17N with bound substrate has also been determined. Taken together, these investigations suggest that the reaction mechanism may proceed through an acyl enzyme intermediate.

X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase.,Thoden JB, Holden HM, Zhuang Z, Dunaway-Mariano D J Biol Chem. 2002 Jul 26;277(30):27468-76. Epub 2002 May 7. PMID:11997398<ref>PMID:11997398</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1lo8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thioesterase|Thioesterase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: 4-hydroxybenzoyl-CoA thioesterase]]
[[Category: Pseuc]]
[[Category: Dunaway-Mariano, D]]
[[Category: Holden, H M]]
[[Category: Thoden, J B]]
[[Category: Zhuang, Z]]
[[Category: Catalytic mechanism]]
[[Category: Hot dog fold]]
[[Category: Hydrolase]]
[[Category: Thioesterase]]