5my0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==KS-MAT DI-DOMAIN OF MOUSE FAS WITH MALONYL-COA== | |
| + | <StructureSection load='5my0' size='340' side='right' caption='[[5my0]], [[Resolution|resolution]] 2.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5my0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MY0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MY0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MLC:MALONYL-COENZYME+A'>MLC</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=K5L:'>K5L</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5my0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5my0 OCA], [http://pdbe.org/5my0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5my0 RCSB], [http://www.ebi.ac.uk/pdbsum/5my0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5my0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FAS_MOUSE FAS_MOUSE]] 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fatty acid synthases (FASs) and polyketide synthases (PKSs) condense acyl compounds to fatty acids and polyketides, respectively. Both, FASs and PKSs, harbor acyltransferases (ATs), which select substrates for condensation by beta-ketoacyl synthases (KSs). Here, we present the structural and functional characterization of the polyspecific malonyl/acetyltransferase (MAT) of murine FAS. We assign kinetic constants for the transacylation of the native substrates, acetyl- and malonyl-CoA, and demonstrate the promiscuity of FAS to accept structurally and chemically diverse CoA-esters. X-ray structural data of the KS-MAT didomain in a malonyl-loaded state suggests a MAT-specific role of an active site arginine in transacylation. Owing to its enzymatic properties and its accessibility as a separate domain, MAT of murine FAS may serve as versatile tool for engineering PKSs to provide custom-tailored access to new polyketides that can be applied in antibiotic and antineoplastic therapy. | ||
| - | + | Characterization of the polyspecific transferase of murine type I fatty acid synthase (FAS) and implications for polyketide synthase (PKS) engineering.,Rittner A, Paithankar KS, Vu Huu K, Grininger M ACS Chem Biol. 2018 Jan 12. doi: 10.1021/acschembio.7b00718. PMID:29328619<ref>PMID:29328619</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5my0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Grininger, M]] | ||
| + | [[Category: Huu, K V]] | ||
| + | [[Category: Paithankar, K S]] | ||
| + | [[Category: Rittner, A]] | ||
| + | [[Category: Mouse fatty-acid-synthase ks-mat malonyl-coa]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 18:21, 24 January 2018
KS-MAT DI-DOMAIN OF MOUSE FAS WITH MALONYL-COA
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