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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qys OCA], [https://pdbe.org/6qys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qys RCSB], [https://www.ebi.ac.uk/pdbsum/6qys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qys ProSAT]</span></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=6qys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qys OCA], [https://pdbe.org/6qys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qys RCSB], [https://www.ebi.ac.uk/pdbsum/6qys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qys ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| In response to the growing threat posed by antibiotic-resistant bacterial strains, extensive research is currently focused on developing antimicrobial agents that target lipid II, a vital precursor in the biosynthesis of bacterial cell walls. The lantibiotic nisin and related peptides display unique and highly selective binding to lipid II. A key feature of the nisin-lipid II interaction is the formation of a cage-like complex between the pyrophosphate moiety of lipid II and the two thioether-bridged rings, rings A and B, at the N-terminus of nisin. To understand the important structural factors underlying this highly selective molecular recognition, we have used solid-phase peptide synthesis to prepare individual ring A and B structures from nisin, the related lantibiotic mutacin, and synthetic analogues. Through NMR studies of these rings, we have demonstrated that ring A is preorganized to adopt the correct conformation for binding lipid II in solution and that individual amino acid substitutions in ring A have little effect on the conformation. We have also analyzed the turn structures adopted by these thioether-bridged peptides and show that they do not adopt the tight alpha-turn or beta-turn structures typically found in proteins.
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| Molecular Recognition of Lipid II by Lantibiotics: Synthesis and Conformational Studies of Analogues of Nisin and Mutacin Rings A and B.,Dickman R, Mitchell SA, Figueiredo AM, Hansen DF, Tabor AB J Org Chem. 2019 Sep 20;84(18):11493-11512. doi: 10.1021/acs.joc.9b01253. Epub , 2019 Aug 29. PMID:31464129<ref>PMID:31464129</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6qys" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
