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| | ==X-ray structure of 4-Hydroxybenzoyl CoA Thioesterase complexed with 4-hydroxyphenacyl CoA== | | ==X-ray structure of 4-Hydroxybenzoyl CoA Thioesterase complexed with 4-hydroxyphenacyl CoA== |
| - | <StructureSection load='1lo7' size='340' side='right' caption='[[1lo7]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='1lo7' size='340' side='right'caption='[[1lo7]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1lo7]] 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=1LO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LO7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1lo7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._CBS3 Pseudomonas sp. CBS3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LO7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CO:4-HYDROXYPHENACYL+COENZYME+A'>4CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lo8|1lo8]], [[1lo9|1lo9]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4CO:4-HYDROXYPHENACYL+COENZYME+A'>4CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lo7 OCA], [https://pdbe.org/1lo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lo7 RCSB], [https://www.ebi.ac.uk/pdbsum/1lo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lo7 ProSAT]</span></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=1lo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lo7 OCA], [http://pdbe.org/1lo7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lo7 RCSB], [http://www.ebi.ac.uk/pdbsum/1lo7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lo7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [https://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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1lo7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1lo7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Thioesterase 3D structures|Thioesterase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-hydroxybenzoyl-CoA thioesterase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pseuc]] | + | [[Category: Pseudomonas sp. CBS3]] |
| - | [[Category: Dunaway-Mariano, D]] | + | [[Category: Dunaway-Mariano D]] |
| - | [[Category: Holden, H M]] | + | [[Category: Holden HM]] |
| - | [[Category: Thoden, J B]] | + | [[Category: Thoden JB]] |
| - | [[Category: Zhuang, Z]] | + | [[Category: Zhuang Z]] |
| - | [[Category: Catalytic mechanism]]
| + | |
| - | [[Category: Hot dog fold]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Thioesterase]]
| + | |
| Structural highlights
Function
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.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chang KH, Liang PH, Beck W, Scholten JD, Dunaway-Mariano D. Isolation and characterization of the three polypeptide components of 4-chlorobenzoate dehalogenase from Pseudomonas sp. strain CBS-3. Biochemistry. 1992 Jun 23;31(24):5605-10. PMID:1610806
- ↑ Thoden JB, Holden HM, Zhuang Z, Dunaway-Mariano D. X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase. J Biol Chem. 2002 Jul 26;277(30):27468-76. Epub 2002 May 7. PMID:11997398 doi:10.1074/jbc.M203904200
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