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TitleThe unusual structure of Ruminococcin C1 antimicrobial peptide confers clinical properties.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 117, Page 19168-19177, Year 2020
Publish dateOct 10, 2019 (structure data deposition date)
AuthorsRoblin, C. / Chiumento, S. / Bornet, O. / Nouailler, M. / Muller, C.S. / Jeannot, K. / Basset, C. / Kieffer-Jaquinod, S. / Coute, Y. / Torelli, S. ...Roblin, C. / Chiumento, S. / Bornet, O. / Nouailler, M. / Muller, C.S. / Jeannot, K. / Basset, C. / Kieffer-Jaquinod, S. / Coute, Y. / Torelli, S. / Le Pape, L. / Schunemann, V. / Olleik, H. / De La Villeon, B. / Sockeel, P. / Di Pasquale, E. / Nicoletti, C. / Vidal, N. / Poljak, L. / Iranzo, O. / Giardina, T. / Fons, M. / Devillard, E. / Polard, P. / Maresca, M. / Perrier, J. / Atta, M. / Guerlesquin, F. / Lafond, M. / Duarte, V.
External linksProc. Natl. Acad. Sci. USA / PubMed:32719135
MethodsNMR (solution)
Structure data

PDB-6t33:
The unusual structure of Ruminococcin C1 antimicrobial peptide confers activity against clinical pathogens
Method: SOLUTION NMR

Source
  • [ruminococcus] gnavus e1 (bacteria)
KeywordsANTIMICROBIAL PROTEIN / bacteriocin / ruminoccin / antibiotic / thioether bridge

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