Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Posttranslational Modifications Linking Cysteine Sulfurs to ttp://pubs.acs.org/i

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• 作者：Karen Kawulka ; Tara Sprules ; Ryan T. McKay ; Pascal Mercier ; Christopher M. Diaper ; Peter Zuber ; and John C. Vederas
• 刊名：Journal of the American Chemical Society
• 出版年：2003
• 出版时间：April 23, 2003
• 年：2003
• 卷：125
• 期：16
• 页码：4726 - 4727
• 全文大小：92K
• 年卷期：v.125,no.16(April 23, 2003)
• ISSN：1520-5126

文摘

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 -positions of Phe22, Thr28, and Phe31, respectively. Such posttranslational linkage of a thiol to the -carbon of an amino acid residue is very unusual in natural peptides or proteins. Subtilosin A (1) belongs to a new class of bacteriocins.