2uv8

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{{Large structure}}
 
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{{STRUCTURE_2uv8| PDB=2uv8 | SCENE= }}
 
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===CRYSTAL STRUCTURE OF YEAST FATTY ACID SYNTHASE WITH STALLED ACYL CARRIER PROTEIN AT 3.1 ANGSTROM RESOLUTION===
 
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{{ABSTRACT_PUBMED_17431182}}
 
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==About this Structure==
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==Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution==
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[[2uv8]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UV8 OCA].
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<StructureSection load='2uv8' size='340' side='right'caption='[[2uv8]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2uv8]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UV8 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]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GVL:O-[(R)-{[(3R)-4-AMINO-3-HYDROXY-2,2-DIMETHYL-4-OXOBUTYL]OXY}(HYDROXY)PHOSPHORYL]-L-SERINE'>GVL</scene></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=2uv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uv8 OCA], [https://pdbe.org/2uv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2uv8 RCSB], [https://www.ebi.ac.uk/pdbsum/2uv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2uv8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FAS2_YEAST FAS2_YEAST] Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.[HAMAP-Rule:MF_00101]
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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/uv/2uv8_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=2uv8 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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In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the Saccharomyces cerevisiae FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.
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==See Also==
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Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase.,Leibundgut M, Jenni S, Frick C, Ban N Science. 2007 Apr 13;316(5822):288-90. PMID:17431182<ref>PMID:17431182</ref>
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*[[Fatty acid synthase|Fatty acid synthase]]
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:017431182</ref><references group="xtra"/>
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</div>
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[[Category: Fatty-acyl-CoA synthase]]
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<div class="pdbe-citations 2uv8" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Fatty acid synthase 3D structures|Fatty acid synthase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Ban, N.]]
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[[Category: Ban N]]
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[[Category: Frick, C.]]
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[[Category: Frick C]]
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[[Category: Jenni, S.]]
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[[Category: Jenni S]]
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[[Category: Leibundgut, M.]]
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[[Category: Leibundgut M]]
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[[Category: Acetyl transferase]]
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[[Category: Acyl carrier protein]]
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[[Category: Dehydratase]]
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[[Category: Enoyl reductase]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Fatty acid synthase]]
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[[Category: Fatty acid synthesis]]
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[[Category: Hydrolase]]
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[[Category: Ketoacyl reductase]]
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[[Category: Ketoacyl synthase]]
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[[Category: Lipid synthesis]]
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[[Category: Lyase]]
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[[Category: Malonyl/palmitoyl transferase]]
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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: Substrate shuttling]]
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[[Category: Transferase]]
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[[Category: Yeast]]
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Current revision

Crystal structure of yeast fatty acid synthase with stalled acyl carrier protein at 3.1 angstrom resolution

PDB ID 2uv8

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Proteopedia Page Contributors and Editors (what is this?)

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