Solution structure of plantaricin C, a novel lantibiotic.
Eur J Biochem, 1999/9;264(3):833-9.
Turner DL[1], Brennan L, Meyer HE, Lohaus C, Siethoff C, Costa HS, Gonzalez B, Santos H, Suárez JE
Affiliations
PMID: 10491130
Abstract
Plantaricin C, a bacteriocin produced by a Lactobacillus plantarum strain of dairy origin, is a lantibiotic. One dehydroalanine, one lanthionine and three beta-methyl-lanthionine residues were found in its 27 amino acid sequence. The plantaricin C structure has two parts: the first comprises the six NH2-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 beta-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 alpha-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.
MeSH terms
Amino Acid Sequence; Anti-Bacterial Agents; Bacteriocins; Lactobacillus; Magnetic Resonance Spectroscopy; Models, Molecular; Peptides; Protein Conformation; Solutions; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Static Electricity
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