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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
Author(s) -
Sit Clarissa S.,
Lohans Christopher T.,
van Belkum Marco J.,
Campbell Chantel D.,
Miskolzie Mark,
Vederas John C.
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100634
Subject(s) - leucine , serine , disulfide bond , substitution (logic) , stereochemistry , bacteriocin , chemistry , bridge (graph theory) , peptide , biochemistry , amino acid , biology , computer science , enzyme , organic chemistry , anatomy , antimicrobial , programming language
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.