6qyu: Difference between revisions
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The | ==Solution NMR of synthetic analogues of nisin and mutacin ring A and ring B - Mutacin I Ring A== | ||
<StructureSection load='6qyu' size='340' side='right'caption='[[6qyu]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6qyu]] 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=6QYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QYU 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>, <scene name='pdbligand=DHA:2-AMINO-ACRYLIC+ACID'>DHA</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=6qyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qyu OCA], [https://pdbe.org/6qyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qyu RCSB], [https://www.ebi.ac.uk/pdbsum/6qyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qyu ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6qyu" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Figueiredo | <references/> | ||
[[Category: Mitchell | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Lactococcus lactis]] | |||
[[Category: Large Structures]] | |||
[[Category: Dickman R]] | |||
[[Category: Figueiredo A]] | |||
[[Category: Hansen DF]] | |||
[[Category: Mitchell SA]] | |||
[[Category: Tabor AB]] | |||
Latest revision as of 14:01, 14 June 2023
Solution NMR of synthetic analogues of nisin and mutacin ring A and ring B - Mutacin I Ring ASolution NMR of synthetic analogues of nisin and mutacin ring A and ring B - Mutacin I Ring A
Structural highlights
Publication Abstract from PubMedIn 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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