View source for 6qyr


==Solution NMR of synthetic analogues of nisin and mutacin ring A and ring B - Mutacin I Ring B, minor conformer==
<StructureSection load='6qyr' size='340' side='right'caption='[[6qyr]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qyr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QYR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</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=6qyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qyr OCA], [https://pdbe.org/6qyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qyr RCSB], [https://www.ebi.ac.uk/pdbsum/6qyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qyr ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6qyr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactococcus lactis]]
[[Category: Large Structures]]
[[Category: Dickman R]]
[[Category: Figueiredo A]]
[[Category: Hansen DF]]
[[Category: Mitchell SA]]
[[Category: Tabor AB]]