6QYV
Solution NMR of synthetic analogues of nisin and mutacin ring A and ring B - Mutacin I Ring A (Ser2, Ala5, Ala8) analogue
Summary for 6QYV
| Entry DOI | 10.2210/pdb6qyv/pdb |
| Related | 1WCO 6QM1 6QTF 6QYR 6QYS 6QYT 6QYU |
| NMR Information | BMRB: 34373 |
| Descriptor | PHE-SER-DAL-LEU-ALA-LEU-CYS-ALA (1 entity in total) |
| Functional Keywords | peptide antibiotic, lantibiotic, antimicrobial, bacteriocin, thioester, antibiotic |
| Biological source | Lactococcus lactis |
| Total number of polymer chains | 1 |
| Total formula weight | 794.96 |
| Authors | Dickman, R.,Mitchell, S.A.,Figueiredo, A.,Hansen, D.F.,Tabor, A.B. (deposition date: 2019-03-09, release date: 2019-09-11, Last modification date: 2024-10-16) |
| Primary citation | Dickman, R.,Mitchell, S.A.,Figueiredo, A.M.,Hansen, D.F.,Tabor, A.B. Molecular Recognition of Lipid II by Lantibiotics: Synthesis and Conformational Studies of Analogues of Nisin and Mutacin Rings A and B. J.Org.Chem., 84:11493-11512, 2019 Cited by PubMed Abstract: 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 α-turn or β-turn structures typically found in proteins. PubMed: 31464129DOI: 10.1021/acs.joc.9b01253 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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