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TitleThe Myxobacterial Antibiotic Myxovalargin: Biosynthesis, Structural Revision, Total Synthesis, and Molecular Characterization of Ribosomal Inhibition.
Journal, issue, pagesJ Am Chem Soc, Vol. 145, Issue 2, Page 851-863, Year 2023
Publish dateJan 18, 2023
AuthorsTimm O Koller / Ullrich Scheid / Teresa Kösel / Jennifer Herrmann / Daniel Krug / Helena I M Boshoff / Bertrand Beckert / Joanna C Evans / Jan Schlemmer / Becky Sloan / Danielle M Weiner / Laura E Via / Atica Moosa / Thomas R Ioerger / Michael Graf / Boris Zinshteyn / Maha Abdelshahid / Fabian Nguyen / Stefan Arenz / Franziska Gille / Maik Siebke / Tim Seedorf / Oliver Plettenburg / Rachel Green / Anna-Luisa Warnke / Joachim Ullrich / Ralf Warrass / Clifton E Barry / Digby F Warner / Valerie Mizrahi / Andreas Kirschning / Daniel N Wilson / Rolf Müller /
PubMed AbstractResistance of bacterial pathogens against antibiotics is declared by WHO as a major global health threat. As novel antibacterial agents are urgently needed, we re-assessed the broad-spectrum ...Resistance of bacterial pathogens against antibiotics is declared by WHO as a major global health threat. As novel antibacterial agents are urgently needed, we re-assessed the broad-spectrum myxobacterial antibiotic myxovalargin and found it to be extremely potent against . To ensure compound supply for further development, we studied myxovalargin biosynthesis in detail enabling production via fermentation of a native producer. Feeding experiments as well as functional genomics analysis suggested a structural revision, which was eventually corroborated by the development of a concise total synthesis. The ribosome was identified as the molecular target based on resistant mutant sequencing, and a cryo-EM structure revealed that myxovalargin binds within and completely occludes the exit tunnel, consistent with a mode of action to arrest translation during a late stage of translation initiation. These studies open avenues for structure-based scaffold improvement toward development as an antibacterial agent.
External linksJ Am Chem Soc / PubMed:36603206 / PubMed Central
MethodsEM (single particle)
Resolution2.1 - 3.0 Å
Structure data

14121

7qq3

EMDB-14121, PDB-7qq3:
Cryo-EM structure of the E.coli 50S ribosomal subunit in complex with the antibiotic Myxovalargin A.
Method: EM (single particle) / Resolution: 2.1 Å

15905

8b7y

EMDB-15905, PDB-8b7y:
Cryo-EM structure of the E.coli 70S ribosome in complex with the antibiotic Myxovalargin B.
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-FME:
N-FORMYLMETHIONINE / N-Formylmethionine

ChemComp-SPD:
SPERMIDINE / Spermidine

Source
  • Escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
  • myxococcus fulvus (bacteria)
  • Escherichia coli BW25113 (bacteria)
KeywordsRIBOSOME / Antibiotic / Myxovalargin A / MyxA / Myxovalargin B / MyxB / fMet-tRNA / P-tRNA

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