2vsu

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[[Image:2vsu.jpg|left|200px]]
 
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==A ternary complex of Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) with acetyl-Coenzyme A and vanillin gives insights into substrate specificity and mechanism.==
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The line below this paragraph, containing "STRUCTURE_2vsu", creates the "Structure Box" on the page.
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<StructureSection load='2vsu' size='340' side='right'caption='[[2vsu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vsu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VSU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=V55:4-HYDROXY-3-METHOXYBENZALDEHYDE'>V55</scene></td></tr>
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{{STRUCTURE_2vsu| PDB=2vsu | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vsu OCA], [https://pdbe.org/2vsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vsu RCSB], [https://www.ebi.ac.uk/pdbsum/2vsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vsu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HCHL_PSEFL HCHL_PSEFL] Catalyzes the hydration of the acyl-CoA thioester of ferulic acid and the subsequent retro-aldol cleavage of the hydrated intermediate to yield vanillin (4-hydroxy-3-methoxy-benzaldehyde).<ref>PMID:9461612</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vs/2vsu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=2vsu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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HCHL (hydroxycinnamoyl-CoA hydratase-lyase) catalyses the biotransformation of feruloyl-CoA to acetyl-CoA and the important flavour-fragrance compound vanillin (4-hydroxy-3-methoxybenzaldehyde) and is exploited in whole-cell systems for the bioconversion of ferulic acid into natural equivalent vanillin. The reaction catalysed by HCHL has been thought to proceed by a two-step process involving first the hydration of the double bond of feruloyl-CoA and then the cleavage of the resultant beta-hydroxy thioester by retro-aldol reaction to yield the products. Kinetic analysis of active-site residues identified using the crystal structure of HCHL revealed that while Glu-143 was essential for activity, Ser-123 played no major role in catalysis. However, mutation of Tyr-239 to Phe greatly increased the K(M) for the substrate ferulic acid, fulfilling its anticipated role as a factor in substrate binding. Structures of WT (wild-type) HCHL and of the S123A mutant, each of which had been co-crystallized with feruloyl-CoA, reveal a subtle helix movement upon ligand binding, the consequence of which is to bring the phenolic hydroxyl of Tyr-239 into close proximity to Tyr-75 from a neighbouring subunit in order to bind the phenolic hydroxyl of the product vanillin, for which electron density was observed. The active-site residues of ligand-bound HCHL display a remarkable three-dimensional overlap with those of a structurally unrelated enzyme, vanillyl alcohol oxidase, that also recognizes p-hydroxylated aromatic substrates related to vanillin. The data both explain the observed substrate specificity of HCHL for p-hydroxylated cinnamate derivatives and illustrate a remarkable convergence of the molecular determinants of ligand recognition between the two otherwise unrelated enzymes.
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'''A TERNARY COMPLEX OF HYDROXYCINNAMOYL-COA HYDRATASE-LYASE (HCHL) WITH ACETYL-COENZYME A AND VANILLIN GIVES INSIGHTS INTO SUBSTRATE SPECIFICITY AND MECHANISM.'''
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A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) with acetyl-CoA and vanillin gives insights into substrate specificity and mechanism.,Bennett JP, Bertin L, Moulton B, Fairlamb IJ, Brzozowski AM, Walton NJ, Grogan G Biochem J. 2008 Sep 1;414(2):281-9. PMID:18479250<ref>PMID:18479250</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==Overview==
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</div>
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Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) catalyses the biotransformation of feruloyl-CoA to acetyl-CoA and the important flavour-fragrance compound vanillin (4-hydroxy 3-methoxybenzaldehyde) and is exploited in whole-cell systems for the bioconversion of ferulic acid to natural-equivalent vanillin. The reaction catalysed by HCHL has been thought to proceed by a two-step process involving first the hydration of the double bond of feruloyl-CoA, then the cleavage of the resultant beta-hydroxy thioester by retro-aldol reaction to yield the products. Kinetic analysis of active site residues identified using the crystal structure of HCHL revealed that whilst Glu-143 was essential for activity, Ser-123 played no major role in catalysis. However, mutation of Tyr-239 to Phe greatly increased the KM for the substrate ferulic acid, fulfilling its anticipated role as a factor in substrate binding. Structures of wild-type HCHL and of the Ser123Ala mutant, each of which had been co-crystallised with feruloyl-CoA, reveal a subtle helix movement upon ligand binding, the consequence of which is to bring the phenolic hydroxyl of Tyr-239 into close proximity with Tyr-75 from a neighbouring subunit in order to bind the phenolic hydroxyl of the product vanillin, for which electron density was observed. The active site residues of ligand-bound HCHL display a remarkable three-dimensional overlap with those of a structurally unrelated enzyme, vanillyl alcohol oxidase, that also recognises para-hydroxylated aromatic substrates related to vanillin. The data both explain the observed substrate specificity of HCHL for para-hydroxylated cinnamate derivatives and illustrate a remarkable convergence of the molecular determinants of ligand recognition between two otherwise unrelated enzymes.
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<div class="pdbe-citations 2vsu" style="background-color:#fffaf0;"></div>
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== References ==
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==About this Structure==
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<references/>
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2VSU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VSU OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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A ternary complex of Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) with acetyl-Coenzyme A and vanillin gives insights into substrate specificity and mechanism., Bennett JP, Bertin L, Moulton B, Fairlamb IJ, Brzozowski AM, Walton NJ, Grogan G, Biochem J. 2008 May 14;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18479250 18479250]
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[[Category: Pseudomonas fluorescens]]
[[Category: Pseudomonas fluorescens]]
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[[Category: Single protein]]
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[[Category: Bennett JP]]
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[[Category: Trans-feruloyl-CoA hydratase]]
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[[Category: Bertin LM]]
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[[Category: Bennett, J P.]]
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[[Category: Brzozowski AM]]
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[[Category: Bertin, L M.]]
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[[Category: Grogan G]]
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[[Category: Brzozowski, A M.]]
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[[Category: Walton NJ]]
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[[Category: Grogan, G.]]
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[[Category: Walton, N J.]]
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[[Category: Aldolase]]
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[[Category: Crotonase]]
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[[Category: Hydratase]]
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[[Category: Lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:17:01 2008''
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Current revision

A ternary complex of Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) with acetyl-Coenzyme A and vanillin gives insights into substrate specificity and mechanism.

PDB ID 2vsu

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