Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Posttranslational Modifications Linking Cysteine Sulfurs to α-Carbons of Phenylalanine and Threonine

29 March 2003

journal article
research article
Published by American Chemical Society (ACS) in Journal of the American Chemical Society

Vol. 125 (16) , 4726-4727
https://doi.org/10.1021/ja029654t

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.

Keywords

This publication has 4 references indexed in Scilit:

Structure of the Bacillus subtilis Peptide Antibiotic Subtilosin A Determined by 1H-NMR and Matrix Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry
Protein Journal, 2001
Nitrogen-15- and carbon-13-labeled media from Anabaena sp. for universal isotopic labeling of bacteriocins: NMR resonance assignments of leucocin A from Leuconostoc gelidum and nisin A from Lactococcus lactis
Biochemistry, 1993
Subtilosin A, a New Antibiotic Peptide Produced by Bacillus subtilis 168: Isolation, Structural Analysis, and Biogenesis1
The Journal of Biochemistry, 1985
The Biosynthesis of Gliotoxin and Related Epipolythiodioxopiperazines
Published by Elsevier ,1980