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==The unusual structure of Ruminococcin C1 antimicrobial peptide confers activity against clinical pathogens==
<StructureSection load='6t33' size='340' side='right'caption='[[6t33]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T33 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6t33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t33 OCA], [https://pdbe.org/6t33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t33 RCSB], [https://www.ebi.ac.uk/pdbsum/6t33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t33 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The emergence of superbugs developing resistance to antibiotics and the resurgence of microbial infections have led scientists to start an antimicrobial arms race. In this context, we have previously identified an active RiPP, the Ruminococcin C1, naturally produced by Ruminococcus gnavus E1, a symbiont of the healthy human intestinal microbiota. This RiPP, subclassified as a sactipeptide, requires the host digestive system to become active against pathogenic Clostridia and multidrug-resistant strains. Here we report its unique compact structure on the basis of four intramolecular thioether bridges with reversed stereochemistry introduced posttranslationally by a specific radical-SAM sactisynthase. This structure confers to the Ruminococcin C1 important clinical properties including stability to digestive conditions and physicochemical treatments, a higher affinity for bacteria than simulated intestinal epithelium, a valuable activity at therapeutic doses on a range of clinical pathogens, mediated by energy resources disruption, and finally safety for human gut tissues.

The unusual structure of Ruminococcin C1 antimicrobial peptide confers clinical properties.,Roblin C, Chiumento S, Bornet O, Nouailler M, Muller CS, 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 Proc Natl Acad Sci U S A. 2020 Jul 27. pii: 2004045117. doi:, 10.1073/pnas.2004045117. PMID:32719135<ref>PMID:32719135</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Atta M]]
[[Category: Basset C]]
[[Category: Bornet O]]
[[Category: Chiumento S]]
[[Category: Coute Y]]
[[Category: Devillard E]]
[[Category: Duarte V]]
[[Category: Fons M]]
[[Category: Giardina T]]
[[Category: Guerlesquin F]]
[[Category: Iranzo O]]
[[Category: Jeannot K]]
[[Category: Kieffer-Jaquinod S]]
[[Category: Lafond M]]
[[Category: Le Pape L]]
[[Category: Maresca M]]
[[Category: Muller C]]
[[Category: Nicoletti C]]
[[Category: Nouailler M]]
[[Category: Perrier J]]
[[Category: Roblin C]]
[[Category: Shunemann V]]
[[Category: Torelli S]]