5z5r
From Proteopedia
Nukacin ISK-1 in inactive state
Structural highlights
FunctionLANNA_STAWA Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria, such as Lactobacillus sakei, Leuconostoc mesenteroides and Pediococcus pentosaceus. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.[1] [2] [REFERENCE:4] Publication Abstract from PubMedThe lantibiotic nukacin ISK-1 exerts antimicrobial activity through binding to lipid II. Here, we perform NMR analyses of the structure of nukacin ISK-1 and the interaction with lipid II. Unexpectedly, nukacin ISK-1 exists in two structural states in aqueous solution, with an interconversion rate on a time scale of seconds. The two structures differ in the relative orientations of the two lanthionine rings, ring A and ring C. Chemical shift perturbation induced by the titration of lipid II reveals that only one state was capable of binding to lipid II. On the molecular surface of the active state, a multiple hydrogen-bonding site formed by amino acid residues in the ring A region is adjacent to a hydrophobic surface formed by residues in the ring C region, and we propose that these sites interact with the pyrophosphate moiety and the isoprene chain of the lipid II molecule, respectively. The lantibiotic nukacin ISK-1 exists in an equilibrium between active and inactive lipid-II binding states.,Fujinami D, -Mahin AA, Elsayed KM, Islam MR, Nagao JI, Roy U, Momin S, Zendo T, Kohda D, Sonomoto K Commun Biol. 2018 Sep 25;1:150. doi: 10.1038/s42003-018-0150-3. eCollection 2018. PMID:30272026[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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