TY - JOUR
T1 - Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine
AU - Kawulka, Karen
AU - Sprules, Tara
AU - McKay, Ryan T.
AU - Mercier, Pascal
AU - Diaper, Christopher M.
AU - Zuber, Peter
AU - Vederas, John C.
PY - 2003/4/23
Y1 - 2003/4/23
N2 - 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.
AB - 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.
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U2 - 10.1021/ja029654t
DO - 10.1021/ja029654t
M3 - Article
C2 - 12696888
AN - SCOPUS:0037462081
SN - 0002-7863
VL - 125
SP - 4726
EP - 4727
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 16
ER -