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

doi:10.1021/ja029654t

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

Center for Coastal Margins

Research output: Contribution to journal › Article › peer-review

101 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 language	English (US)
Pages (from-to)	4726-4727
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	125
Issue number	16
DOIs	https://doi.org/10.1021/ja029654t
State	Published - Apr 23 2003

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja029654t

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Kawulka, K., Sprules, T., McKay, R. T., Mercier, P., Diaper, C. M., Zuber, P., & Vederas, J. C. (2003). Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine. Journal of the American Chemical Society, 125(16), 4726-4727. https://doi.org/10.1021/ja029654t

Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine. / Kawulka, Karen; Sprules, Tara; McKay, Ryan T. et al.

In: Journal of the American Chemical Society, Vol. 125, No. 16, 23.04.2003, p. 4726-4727.

Research output: Contribution to journal › Article › peer-review

Kawulka, K, Sprules, T, McKay, RT, Mercier, P, Diaper, CM, Zuber, P & Vederas, JC 2003, 'Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine', Journal of the American Chemical Society, vol. 125, no. 16, pp. 4726-4727. https://doi.org/10.1021/ja029654t

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

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.",

author = "Karen Kawulka and Tara Sprules and McKay, {Ryan T.} and Pascal Mercier and Diaper, {Christopher M.} and Peter Zuber and Vederas, {John C.}",

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

Abstract

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