The 3D Solution Structure of Thurincin H, a Bacteriocin with Four Sulfur to α‐Carbon Crosslinks
Author(s) -
Sit Clarissa S.,
van Belkum Marco J.,
McKay Ryan T.,
Worobo Randy W.,
Vederas John C.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201102527
Subject(s) - bacteriocin , thioether , chemistry , sulfur , schematic , peptide , combinatorial chemistry , stereochemistry , antimicrobial , organic chemistry , biochemistry , electronic engineering , engineering
Problem solved : Thurincin H is an antimicrobial peptide with suspected post‐translational modifications. MS/MS sequencing identified the residues that were modified, and NMR spectroscopic studies in solution led to the 3D structure of thurincin H, which features four SC α thioether crosslinks (yellow in schematic representation). This structure may be representative of several other bacteriocins with identical masses.