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| | ==Solution structure of OlvA(BC)== | | ==Solution structure of OlvA(BC)== |
| - | <StructureSection load='6pqg' size='340' side='right'caption='[[6pqg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6pqg' size='340' side='right'caption='[[6pqg]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6pqg]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PQG FirstGlance]. <br> | + | <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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=6pqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pqg OCA], [http://pdbe.org/6pqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pqg RCSB], [http://www.ebi.ac.uk/pdbsum/6pqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pqg ProSAT]</span></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> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Acedo, J Z]] | + | [[Category: Streptomyces olivaceus]] |
| - | [[Category: Donk, W A.van der]] | + | [[Category: Acedo JZ]] |
| - | [[Category: Lanthipeptide]] | + | [[Category: Van der Donk WA]] |
| - | [[Category: Ribosomal protein]]
| + | |
| - | [[Category: Ripp]]
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| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Acedo JZ, Bothwell IR, An L, Trouth A, Frazier C, van der Donk WA. O-Methyltransferase-Mediated Incorporation of a beta-Amino Acid in Lanthipeptides. J Am Chem Soc. 2019 Oct 15. doi: 10.1021/jacs.9b07396. PMID:31568727 doi:http://dx.doi.org/10.1021/jacs.9b07396
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