1mka

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==E. COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE MODIFIED BY ITS CLASSIC MECHANISM-BASED INACTIVATOR, 3-DECYNOYL-N-ACETYL CYSTEAMINE==
==E. COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE MODIFIED BY ITS CLASSIC MECHANISM-BASED INACTIVATOR, 3-DECYNOYL-N-ACETYL CYSTEAMINE==
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<StructureSection load='1mka' size='340' side='right' caption='[[1mka]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='1mka' size='340' side='right'caption='[[1mka]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1mka]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MKA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1mka]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKA FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAC:2-DECENOYL+N-ACETYL+CYSTEAMINE'>DAC</scene><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]] 2&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=DAC:2-DECENOYL+N-ACETYL+CYSTEAMINE'>DAC</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxydecanoyl-[acyl-carrier-protein]_dehydratase 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.60 4.2.1.60] </span></td></tr>
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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=1mka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mka OCA], [https://pdbe.org/1mka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mka RCSB], [https://www.ebi.ac.uk/pdbsum/1mka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mka ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mka OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mka RCSB], [http://www.ebi.ac.uk/pdbsum/1mka PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/FABA_ECOLI FABA_ECOLI] Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP.<ref>PMID:8910376</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mk/1mka_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mk/1mka_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=1mka ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 1mka" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Beta-hydroxyacyl-acyl carrier protein dehydratase|Beta-hydroxyacyl-acyl carrier protein dehydratase]]
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*[[Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures|Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Leesong, M.]]
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[[Category: Large Structures]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Leesong M]]

Current revision

E. COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE MODIFIED BY ITS CLASSIC MECHANISM-BASED INACTIVATOR, 3-DECYNOYL-N-ACETYL CYSTEAMINE

PDB ID 1mka

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