Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine

Karen Kawulka, Tara Sprules, Ryan T. McKay, Pascal Mercier, Christopher M. Diaper, Peter Zuber, John C. Vederas

Research output: Contribution to journalArticle

82 Scopus citations

Abstract

The complete primary and three-dimensional solution structures of subtilosin A (1), a bacteriocin from Bacillus subtilis, were determined by multidimensional NMR studies on peptide produced using isotopically labeled [13C,15N]medium derived from Anabaena sp. grown on sodium [13C]bicarbonate and [15N]nitrate. Additional samples of 1 were also generated by separate incorporations of [U-13C,15N]phenylalanine and [U-13C,15N]threonine using otherwise unlabeled media. The results demonstrate that in addition to having a cyclized peptide backbone (N and C termini), three cross-links are formed between the sulfurs of Cys13, Cys7, and Cys4 and the α-positions of Phe22, Thr28, and Phe31, respectively. Such posttranslational linkage of a thiol to the α-carbon of an amino acid residue is very unusual in natural peptides or proteins. Subtilosin A (1) belongs to a new class of bacteriocins.

Original languageEnglish (US)
Pages (from-to)4726-4727
Number of pages2
JournalJournal of the American Chemical Society
Volume125
Issue number16
DOIs
StatePublished - Apr 23 2003

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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