Substitution of a Conserved Disulfide in the Type IIa Bacteriocin, Leucocin A, with L-Leucine and L-Serine Residues: Effects on Activity and Three-Dimensional Structure

• Published in: Chembiochem : a European journal of chemical biology Vol. 13; no. 1; pp. 35 - 38
• Main Authors: Sit, Clarissa S., Lohans, Christopher T., van Belkum, Marco J., Campbell, Chantel D., Miskolzie, Mark, Vederas, John C.
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 02-01-2012; WILEY‐VCH Verlag
• Subjects: bacteriocin; Bacteriocins - chemistry; Bacteriocins - genetics; Bacteriocins - pharmacology; Carnobacterium - drug effects; disulfide substitution; Disulfides - chemistry; Disulfides - metabolism; Leucine - chemistry; leucocin A; Leuconostoc gelidum; Microbial Sensitivity Tests; Models, Molecular; Molecular Structure; Mutation; peptides; Serine - chemistry
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.201100634

Bridge not required: The disulfide bridge in the antibacterial peptide leucocin A was replaced with two Ser or two Leu residues. The double leucine mutant was found to be active, and elucidation of its 3D structure showed that the two leucines interact to hold the N‐ and C‐terminal domains together.