2jfd

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[[Image:2jfd.gif|left|200px]]
 
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{{Structure
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==Structure of the MAT domain of human FAS==
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|PDB= 2jfd |SIZE=350|CAPTION= <scene name='initialview01'>2jfd</scene>, resolution 2.81&Aring;
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<StructureSection load='2jfd' size='340' side='right'caption='[[2jfd]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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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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|ACTIVITY= [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]
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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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|GENE=
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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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}}
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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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==Disease==
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==See Also==
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Known diseases associated with this structure: Autoimmune lymphoproliferative syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134637 134637]], Autoimmune lymphoproliferative syndrome, type IA OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134637 134637]], Squamous cell carcinoma, burn scar-related, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=134637 134637]]
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*[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2JFD is a [[Single protein]] structure of 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=2JFD OCA].
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__TOC__
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[[Category: Fatty-acid synthase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C H.]]
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[[Category: Arrowsmith CH]]
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[[Category: Bunkoczi, G.]]
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[[Category: Bunkoczi G]]
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[[Category: Edwards, A.]]
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[[Category: Edwards A]]
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[[Category: Hozjan, V.]]
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[[Category: Hozjan V]]
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[[Category: Kavanagh, K.]]
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[[Category: Kavanagh K]]
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[[Category: Oppermann, U.]]
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[[Category: Oppermann U]]
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[[Category: Rojkova, A.]]
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[[Category: Rojkova A]]
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[[Category: Smith, S.]]
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[[Category: Smith S]]
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[[Category: Sundstrom, M.]]
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[[Category: Sundstrom M]]
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[[Category: Weigelt, J.]]
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[[Category: Weigelt J]]
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[[Category: Wu, X.]]
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[[Category: Wu X]]
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[[Category: acetyl transferase]]
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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 Thu Mar 20 17:41:11 2008''
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Current revision

Structure of the MAT domain of human FAS

PDB ID 2jfd

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