Open AccessSolution structure of plantaricin C, a novel lantibiotic
Author(s) -
Turner David L.,
Brennan Lorraine,
Meyer Helmut E.,
Lohaus Christiane,
Siethoff Christoph,
Costa Helena S.,
Gonzalez Beatriz,
Santos Helena,
Suárez Juan E.
Publication year - 1999
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1999.00674.x
Subject(s) - lanthionine , lantibiotics , dehydroalanine , nisin , bacteriocin , chemistry , residue (chemistry) , stereochemistry , amino acid , peptide sequence , amphiphile , peptide , biochemistry , organic chemistry , gene , antimicrobial , copolymer , polymer
Plantaricin C, a bacteriocin produced by a Lactobacillus plantarum strain of dairy origin, is a lantibiotic. One dehydroalanine, one lanthionine and three β‐methyl‐lanthionine residues were found in its 27 amino acid sequence. The plantaricin C structure has two parts: the first comprises the six NH 2 ‐terminal residues, four of which are lysines, which confer a strong positive charge to this stretch. The amino acids in positions 7 and 27 form the lanthionine bridge, giving a globular conformation to the rest of the molecule. The β‐methyl‐lanthionine bridges are established between residues 12–15, 13–18 and 23–26. This central region has a charge distribution compatible with an amphipathic α‐helix, through which plantaricin C would become inserted into the membrane matrix of sensitive organisms, provoking the opening of pores and leakage of the cytoplasmic content.