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6pqg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of OlvA(BC)== | |
| + | <StructureSection load='6pqg' size='340' side='right'caption='[[6pqg]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6pqg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_olivaceus Streptomyces olivaceus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PQG FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</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=6pqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pqg OCA], [https://pdbe.org/6pqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pqg RCSB], [https://www.ebi.ac.uk/pdbsum/6pqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pqg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lanthipeptides represent a large class of cyclic natural products defined by the presence of lanthionine (Lan) and methyllanthionine (MeLan) cross-links. With the advances in DNA sequencing technologies and genome mining tools, new biosynthetic enzymes capable of installing unusual structural features are continuously being discovered. In this study, we investigated an O-methyltransferase that is a member of the most prominent auxiliary enzyme family associated with class I lanthipeptide biosynthetic gene clusters. Despite the prevalence of these enzymes, their function has not been established. Herein, we demonstrate that the O-methyltransferase OlvSA encoded in the olv gene cluster from Streptomyces olivaceus NRRL B-3009 catalyzes the rearrangement of a highly conserved aspartate residue to a beta-amino acid, isoaspartate, in the lanthipeptide OlvA(BCSA). We elucidated the NMR solution structure of the GluC-digested peptide, OlvA(BCSA)(GluC), which revealed a unique ring topology comprising four interlocking rings and positions the isoaspartate residue in a solvent exposed loop that is stabilized by a MeLan ring. Gas chromatography-mass spectrometry analysis further indicated that OlvA(BCSA) contains two dl-MeLan rings and two Lan rings with an unusual ll-stereochemistry. Lastly, in vitro reconstitution of OlvSA activity showed that it is a leader peptide-independent and S-adenosyl methionine-dependent O-methyltransferase that mediates the conversion of a highly conserved aspartate residue in a cyclic substrate into a succinimide, which is hydrolyzed to generate an Asp or isoAsp containing peptide. This overall transformation converts an alpha-amino acid into a beta-amino acid in a ribosomally synthesized peptide, via an electrophilic intermediate that may be the intended product. | ||
| - | + | O-Methyltransferase-Mediated Incorporation of a beta-Amino Acid in Lanthipeptides.,Acedo JZ, Bothwell IR, An L, Trouth A, Frazier C, van der Donk WA J Am Chem Soc. 2019 Oct 15. doi: 10.1021/jacs.9b07396. PMID:31568727<ref>PMID:31568727</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Acedo | + | <div class="pdbe-citations 6pqg" style="background-color:#fffaf0;"></div> |
| - | [[Category: Van | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces olivaceus]] | ||
| + | [[Category: Acedo JZ]] | ||
| + | [[Category: Van der Donk WA]] | ||
Current revision
Solution structure of OlvA(BC)
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