4lcm: Difference between revisions

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 ==Simvastatin Synthase (LOVD), from Aspergillus Terreus, LovD9 mutant (simh9014)==
-<StructureSection load='4lcm' size='340' side='right' caption='[[4lcm]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
+<StructureSection load='4lcm' size='340' side='right'caption='[[4lcm]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4lcm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspte Aspte]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LCM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4lcm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_terreus Aspergillus terreus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LCM FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hl9|3hl9]], [[3hlb|3hlb]], [[3hlc|3hlc]], [[3hld|3hld]], [[3hle|3hle]], [[3hlf|3hlf]], [[3hlg|3hlg]], [[4lcl|4lcl]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.19&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lovD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33178 ASPTE])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lcm OCA], [https://pdbe.org/4lcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lcm RCSB], [https://www.ebi.ac.uk/pdbsum/4lcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lcm ProSAT]</span></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=4lcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lcm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lcm RCSB], [http://www.ebi.ac.uk/pdbsum/4lcm PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/LOVD_ASPTE LOVD_ASPTE] Monacolin J acid methylbutanoyltransferase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) (PubMed:10334994, PubMed:12929390, PubMed:21495633). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units (PubMed:10334994, PubMed:10381407, PubMed:19900898, PubMed:22733743). Dihydromonacolin L acid is released from lovB by the thioesterase lovG (PubMed:23653178). Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid (PubMed:12929390, PubMed:21495633). The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit (PubMed:19530726, PubMed:21069965). Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin (PubMed:10334994, PubMed:17113998, PubMed:18988191, PubMed:19875080, PubMed:24727900). LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro (PubMed:19875080). LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates (PubMed:21069965).<ref>PMID:10334994</ref> <ref>PMID:10381407</ref> <ref>PMID:12929390</ref> <ref>PMID:17113998</ref> <ref>PMID:18988191</ref> <ref>PMID:19530726</ref> <ref>PMID:19875080</ref> <ref>PMID:19900898</ref> <ref>PMID:21069965</ref> <ref>PMID:21495633</ref> <ref>PMID:22733743</ref> <ref>PMID:23653178</ref> <ref>PMID:24727900</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4lcm" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Simvastatin Synthase|Simvastatin Synthase]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Aspte]]
+[[Category: Aspergillus terreus]]
-[[Category: Gao, X]]
+[[Category: Large Structures]]
-[[Category: Sawaya, M R]]
+[[Category: Gao X]]
-[[Category: Tang, Y]]
+[[Category: Sawaya MR]]
-[[Category: Yeates, T O]]
+[[Category: Tang Y]]
-[[Category: Laboratory-directed evolution]]
+[[Category: Yeates TO]]
-[[Category: Transesterase]]
-[[Category: Transferase]]