2iwy

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[[Image:2iwy.png|left|200px]]
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==HUMAN MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE==
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<StructureSection load='2iwy' size='340' side='right' caption='[[2iwy]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2iwy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IWY FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c9h|2c9h]], [[2iwz|2iwz]], [[2ix4|2ix4]]</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/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41] </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=2iwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2iwy RCSB], [http://www.ebi.ac.uk/pdbsum/2iwy PDBsum]</span></td></tr>
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<table>
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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/iw/2iwy_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/chain_selection.php?pdb_ID=2ata 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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Two distinct ways of organizing fatty acid biosynthesis exist: the multifunctional type I fatty acid synthase (FAS) of mammals, fungi, and lower eukaryotes with activities residing on one or two polypeptides; and the dissociated type II FAS of prokaryotes, plastids, and mitochondria with individual activities encoded by discrete genes. The beta-ketoacyl [ACP] synthase (KAS) moiety of the mitochondrial FAS (mtKAS) is targeted by the antibiotic cerulenin and possibly by the other antibiotics inhibiting prokaryotic KASes: thiolactomycin, platensimycin, and the alpha-methylene butyrolactone, C75. The high degree of structural similarity between mitochondrial and prokaryotic KASes complicates development of novel antibiotics targeting prokaryotic KAS without affecting KAS domains of cytoplasmic FAS. KASes catalyze the C(2) fatty acid elongation reaction using either a Cys-His-His or Cys-His-Asn catalytic triad. Three KASes with different substrate specificities participate in synthesis of the C(16) and C(18) products of prokaryotic FAS. By comparison, mtKAS carries out all elongation reactions in the mitochondria. We present the X-ray crystal structures of the Cys-His-His-containing human mtKAS and its hexanoyl complex plus the hexanoyl complex of the plant mtKAS from Arabidopsis thaliana. The structures explain (1) the bimodal (C(6) and C(10)-C(12)) substrate preferences leading to the C(8) lipoic acid precursor and long chains for the membranes, respectively, and (2) the low cerulenin sensitivity of the human enzyme; and (3) reveal two different potential acyl-binding-pocket extensions. Rearrangements taking place in the active site, including subtle changes in the water network, indicate a change in cooperativity of the active-site histidines upon primer binding.
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{{STRUCTURE_2iwy| PDB=2iwy | SCENE= }}
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Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase.,Christensen CE, Kragelund BB, von Wettstein-Knowles P, Henriksen A Protein Sci. 2007 Feb;16(2):261-72. PMID:17242430<ref>PMID:17242430</ref>
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===HUMAN MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE===
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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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{{ABSTRACT_PUBMED_17242430}}
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==About this Structure==
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[[2iwy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWY OCA].
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==See Also==
==See Also==
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:017242430</ref><ref group="xtra">PMID:015668256</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 10:08, 29 September 2014

HUMAN MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE

2iwy, resolution 2.06Å

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