8rww
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of native alpha-keto C-methyl transferase SgvM bound to ketoleucine== | |
| + | <StructureSection load='8rww' size='340' side='right'caption='[[8rww]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8rww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseoviridis Streptomyces griseoviridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RWW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COI:2-OXO-4-METHYLPENTANOIC+ACID'>COI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8rww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rww OCA], [https://pdbe.org/8rww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rww RCSB], [https://www.ebi.ac.uk/pdbsum/8rww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rww ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/R9UTR3_STRGD R9UTR3_STRGD] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sâadenosyl-l-methionine-dependent methyltransferases (MTs) are involved in the C-methylation of a variety of natural products. The MTs SgvM from Streptomyces griseoviridis and MrsA from Pseudomonas syringae pv. syringae catalyze the methylation of the beta-carbon atom of alpha-keto acids in the biosynthesis of the antibiotic natural products viridogrisein and 3âmethylarginine, respectively. MrsA shows high substrate selectivity for 5âguanidino-2-oxovalerate, while other alpha-keto acids, such as the SgvM substrates 4-methyl-2-oxovalerate, 2-oxovalerate, and phenylpyruvate, are not accepted. Here we report the crystal structures of SgvM and MrsA in the apo form bound with substrate or Sâadenosyl-l-methionine. By investigating key residues for substrate recognition in the active sites of both enzymes and engineering MrsA by site-directed mutagenesis, the substrate range of MrsA was extended to accept alphaâketo acid substrates of SgvM with uncharged and lipophilic betaâresidues. Our results showcase the transfer of the substrate scope of alpha-keto acid MTs from different biosynthetic pathways by rational design. | ||
| - | + | Structures and protein engineering of the alpha-keto acid C-methyltransferases SgvM and MrsA for rational substrate transfer.,Sommer-Kamann C, Breiltgens J, Zou Z, Gerhardt S, Saleem-Batcha R, Kemper F, Einsle O, Andexer JN, Muller M Chembiochem. 2024 Jun 18:e202400258. doi: 10.1002/cbic.202400258. PMID:38887142<ref>PMID:38887142</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8rww" style="background-color:#fffaf0;"></div> |
| - | [[Category: Andexer | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces griseoviridis]] | ||
| + | [[Category: Andexer JN]] | ||
| + | [[Category: Gerhardt S]] | ||
Current revision
Crystal structure of native alpha-keto C-methyl transferase SgvM bound to ketoleucine
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