1mkb

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(New page: 200px<br /> <applet load="1mkb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mkb, resolution 2.0&Aring;" /> '''ESCHERICHIA COLI BET...)
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[[Image:1mkb.gif|left|200px]]<br />
 
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<applet load="1mkb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mkb, resolution 2.0&Aring;" />
 
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'''ESCHERICHIA COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE AT PH 5 AND 21 DEGREES C'''<br />
 
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==Overview==
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==ESCHERICHIA COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE AT PH 5 AND 21 DEGREES C==
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BACKGROUND. Escherichia coli beta-hydroxydecanoyl thiol ester dehydrase, (dehydrase) is essential to the biosynthesis of unsaturated fatty acids, by shunting a 10-carbon intermediate from the saturated fatty acid pathway, into the unsaturated fatty acid pathway. Dehydrase catalyzes reactions of, dehydration and of double-bond isomerization on 10-carbon thiol esters of, acyl carrier protein (ACP). The aim of this work is to elucidate, mechanisms for the two enzymatic reactions, which occur in an unusual, bifunctional active site, and to understand the specificity of the enzyme, for substrates with 10-carbon fatty acyl chains. RESULTS. Crystal, structures at 2.0 A resolution for free dehydrase and for the enzyme, modified by its classic, mechanism-based inactivator, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8805534 (full description)]]
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<StructureSection load='1mkb' size='340' side='right'caption='[[1mkb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mkb]] 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=1MKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MKB 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]] 2&#8491;</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=1mkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mkb OCA], [https://pdbe.org/1mkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mkb RCSB], [https://www.ebi.ac.uk/pdbsum/1mkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mkb ProSAT]</span></td></tr>
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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>
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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/mk/1mkb_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=1mkb ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MKB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.60 4.2.1.60]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MKB OCA]].
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*[[Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures|Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site., Leesong M, Henderson BS, Gillig JR, Schwab JM, Smith JL, Structure. 1996 Mar 15;4(3):253-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805534 8805534]
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Leesong, M.]]
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[[Category: Leesong M]]
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[[Category: fatty acid biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:35:53 2007''
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Current revision

ESCHERICHIA COLI BETA-HYDROXYDECANOYL THIOL ESTER DEHYDRASE AT PH 5 AND 21 DEGREES C

PDB ID 1mkb

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