3kv8

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[[Image:3kv8.png|left|200px]]
 
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==Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - Wild type FlK in complex with fluoro-acetate==
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The line below this paragraph, containing "STRUCTURE_3kv8", creates the "Structure Box" on the page.
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<StructureSection load='3kv8' size='340' side='right'caption='[[3kv8]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[3kv8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KV8 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.85&#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=FAH:FLUOROACETIC+ACID'>FAH</scene></td></tr>
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{{STRUCTURE_3kv8| PDB=3kv8 | 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=3kv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kv8 OCA], [https://pdbe.org/3kv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kv8 RCSB], [https://www.ebi.ac.uk/pdbsum/3kv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kv8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FLK_STRCT FLK_STRCT] Hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance. Can not use acetyl-CoA as substrate.<ref>PMID:16720268</ref> <ref>PMID:20836570</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/kv/3kv8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3kv8 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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The thioesterase FlK from the fluoroacetate-producing Streptomyces cattleya catalyzes the hydrolysis of fluoroacetyl-coenzyme A. This provides an effective self-defense mechanism, preventing any fluoroacetyl-coenzyme A formed from being further metabolized to 4-hydroxy-trans-aconitate, a lethal inhibitor of the tricarboxylic acid cycle. Remarkably, FlK does not accept acetyl-coenzyme A as a substrate. Crystal structure analysis shows that FlK forms a dimer, in which each subunit adopts a hot dog fold as observed for type II thioesterases. Unlike other type II thioesterases, which invariably utilize either an aspartate or a glutamate as catalytic base, we show by site-directed mutagenesis and crystallography that FlK employs a catalytic triad composed of Thr(42), His(76), and a water molecule, analogous to the Ser/Cys-His-acid triad of type I thioesterases. Structural comparison of FlK complexed with various substrate analogues suggests that the interaction between the fluorine of the substrate and the side chain of Arg(120) located opposite to the catalytic triad is essential for correct coordination of the substrate at the active site and therefore accounts for the substrate specificity.
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===Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - Wild type FlK in complex with fluoro-acetate===
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Structural basis for the activity and substrate specificity of fluoroacetyl-CoA thioesterase FlK.,Dias MV, Huang F, Chirgadze DY, Tosin M, Spiteller D, Dry EF, Leadlay PF, Spencer JB, Blundell TL J Biol Chem. 2010 Jul 16;285(29):22495-504. Epub 2010 Apr 29. PMID:20430898<ref>PMID:20430898</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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</div>
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<div class="pdbe-citations 3kv8" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20430898}}, adds the Publication Abstract to the page
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*[[Thioesterase 3D structures|Thioesterase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20430898 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20430898}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3kv8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_cattleya Streptomyces cattleya]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KV8 OCA].
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==Reference==
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<ref group="xtra">PMID:20430898</ref><references group="xtra"/>
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[[Category: Streptomyces cattleya]]
[[Category: Streptomyces cattleya]]
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[[Category: Blundell, T L.]]
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[[Category: Blundell TL]]
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[[Category: Chirgadze, D Y.]]
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[[Category: Chirgadze DY]]
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[[Category: Dias, M V.B.]]
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[[Category: Dias MVB]]
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[[Category: Huang, F.]]
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[[Category: Huang F]]
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[[Category: Leadlay, P F.]]
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[[Category: Leadlay PF]]
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[[Category: Spencer, J B.]]
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[[Category: Spencer JB]]
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[[Category: Spiteller, D]]
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[[Category: Spiteller D]]
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[[Category: Tosin, M.]]
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[[Category: Tosin M]]
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[[Category: Valentine, E F.]]
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[[Category: Valentine EF]]
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[[Category: Fluoroacetyl-coa thioesterase flk]]
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[[Category: Hot-dog folding]]
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[[Category: Hydrolase]]
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[[Category: Thioesterase]]
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Current revision

Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase FlK - Wild type FlK in complex with fluoro-acetate

PDB ID 3kv8

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