6ix9: Difference between revisions

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-'''Unreleased structure'''
-The entry 6ix9 is ON HOLD  until Paper Publication
+==The structure of LepI C52A in complex with SAM and leporin C==
+<StructureSection load='6ix9' size='340' side='right'caption='[[6ix9]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ix9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IX9 FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B0O:(6R,6aS,10S,10aR)-10-methyl-4-phenyl-6-[(1E)-prop-1-en-1-yl]-2,6,6a,7,8,9,10,10a-octahydro-1H-[2]benzopyrano[4,3-c]pyridin-1-one'>B0O</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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=6ix9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ix9 OCA], [http://pdbe.org/6ix9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ix9 RCSB], [http://www.ebi.ac.uk/pdbsum/6ix9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ix9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/LEPI_ASPFN LEPI_ASPFN]] O-methyltransferase; part of the gene cluster 23 that mediates the biosynthesis of a family of 2-pyridones known as leporins (PubMed:20447271, PubMed:26051490). The hybrid PKS-NRPS synthetase lepA and the enoyl reductase lepG are responsible for fusion of phenylalanine with a hexaketide and subsequent release of the stable tetramic acid precursor, pre-leporin C (PubMed:26051490). Because lepA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase lepG (PubMed:26051490). It is possible that the dehydrogenase lepF also participates in production of pre-leporin C (PubMed:26051490). Cytochrome P450 monooxygenase lepH is then required for the ring expansion step to yield leporin C (PubMed:26051490). Leporin C is then presumably further oxidized by the N-hydroxylase lepD to form leporin B (PubMed:26051490). LepI may possess a function in biosynthesis upstream of lepA (PubMed:26051490). Leporin B is further oxidized in the presence of ferric ion to give the leporin B trimer-iron chelate, but whether or not this reaction is catalyzed by an enzyme in the pathway or by ferric ion is not determined yet (PubMed:26051490).<ref>PMID:26051490</ref> <ref>PMID:20447271</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Cai, Y]]
+[[Category: Hai, Y]]
+[[Category: Ohashi, M]]
+[[Category: Tang, Y]]
+[[Category: Zhou, J]]
+[[Category: Biosynthetic protein]]
+[[Category: Leporin]]
+[[Category: O-methyltransferase]]
+[[Category: Pericyclase]]
+[[Category: Sam]]