2jfd

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{{Seed}}
 
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[[Image:2jfd.png|left|200px]]
 
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==Structure of the MAT domain of human FAS==
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The line below this paragraph, containing "STRUCTURE_2jfd", creates the "Structure Box" on the page.
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<StructureSection load='2jfd' size='340' side='right'caption='[[2jfd]], [[Resolution|resolution]] 2.81&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'>[[2jfd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2JFD 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]] 2.81&#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=2jfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jfd OCA], [https://pdbe.org/2jfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jfd RCSB], [https://www.ebi.ac.uk/pdbsum/2jfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jfd ProSAT]</span></td></tr>
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{{STRUCTURE_2jfd| PDB=2jfd | SCENE= }}
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</table>
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== Function ==
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[https://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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== 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/main_output.php?pdb_ID=2jfd 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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===STRUCTURE OF THE MAT DOMAIN OF HUMAN FAS===
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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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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 2jfd" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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2JFD is a 4 chains structure of sequences 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=2JFD OCA].
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*[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]]
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[[Category: Fatty-acid synthase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Large Structures]]
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[[Category: Bunkoczi, G.]]
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[[Category: Arrowsmith CH]]
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[[Category: Edwards, A.]]
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[[Category: Bunkoczi G]]
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[[Category: Hozjan, V.]]
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[[Category: Edwards A]]
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[[Category: Kavanagh, K.]]
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[[Category: Hozjan V]]
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[[Category: Oppermann, U.]]
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[[Category: Kavanagh K]]
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[[Category: Rojkova, A.]]
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[[Category: Oppermann U]]
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[[Category: Smith, S.]]
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[[Category: Rojkova A]]
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[[Category: Sundstrom, M.]]
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[[Category: Smith S]]
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[[Category: Weigelt, J.]]
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[[Category: Sundstrom M]]
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[[Category: Wu, X.]]
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[[Category: Weigelt J]]
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[[Category: Acetyl transferase]]
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[[Category: Wu X]]
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[[Category: Acetylation]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Fatty acid synthase]]
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[[Category: Hydrolase]]
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[[Category: Lipid synthesis]]
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[[Category: Lyase]]
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[[Category: Malonyl transferase]]
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[[Category: Mat domain]]
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[[Category: Multifunctional enzyme]]
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[[Category: Nad]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Phosphopantetheine]]
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[[Category: Phosphorylation]]
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[[Category: Pyridoxal phosphate]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 01:48:29 2009''
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Current revision

Structure of the MAT domain of human FAS

PDB ID 2jfd

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