2jfd

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{{STRUCTURE_2jfd| PDB=2jfd | SCENE= }}
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==Structure of the MAT domain of human FAS==
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===Structure of the MAT domain of human FAS===
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<StructureSection load='2jfd' size='340' side='right' caption='[[2jfd]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
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{{ABSTRACT_PUBMED_19549604}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2jfd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JFD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JFD FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xkt|1xkt]], [[2cg5|2cg5]]</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/Fatty-acid_synthase Fatty-acid synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.85 2.3.1.85] </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=2jfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2jfd RCSB], [http://www.ebi.ac.uk/pdbsum/2jfd 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/jf/2jfd_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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Animals employ two systems for the de novo biosynthesis of fatty acids: a megasynthase complex in the cytosol (type I) that produces mainly palmitate, and an ensemble of freestanding enzymes in the mitochondria (type II) that produces mainly octanoyl moieties. The acyltransferases responsible for initiation of fatty acid biosynthesis in the two compartments are distinguished by their different substrate specificities: the type I enzyme transfers both the acetyl primer and the malonyl chain extender, whereas the type II enzyme is responsible for translocation of only the malonyl substrate. Crystal structures for the type I and II enzymes, supported by in silico substrate docking studies and mutagenesis experiments that alter their respective specificities, reveal that, although the two enzymes adopt a similar overall fold, subtle differences at their catalytic centers account for their different specificities.
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==Function==
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Structural basis for different specificities of acyltransferases associated with the human cytosolic and mitochondrial fatty acid synthases.,Bunkoczi G, Misquitta S, Wu X, Lee WH, Rojkova A, Kochan G, Kavanagh KL, Oppermann U, Smith S Chem Biol. 2009 Jun 26;16(6):667-75. doi: 10.1016/j.chembiol.2009.04.011. PMID:19549604<ref>PMID:19549604</ref>
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[[http://www.uniprot.org/uniprot/FAS_HUMAN FAS_HUMAN]] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[2jfd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JFD OCA].
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</div>
==See Also==
==See Also==
*[[Fatty acid synthase|Fatty acid synthase]]
*[[Fatty acid synthase|Fatty acid synthase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:019549604</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Fatty-acid synthase]]
[[Category: Fatty-acid synthase]]
[[Category: Human]]
[[Category: Human]]

Revision as of 05:22, 3 October 2014

Structure of the MAT domain of human FAS

2jfd, resolution 2.81Å

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