Sequence‐specific resonance assignment and conformational analysis of subtilin by 2D NMR

FEBS Letters

Yang, J.C.¹  Leyland, Mark L.¹  Chan, Weng C.²  Bycroft, Barrie W.²  Lian, Lu-Yun¹  Roberts, Gordon C.K.¹ 

[1] Biological NMR Centre and Department of Biochemistry, University of Leicester, Leicester, LE1 9HN, UK;Department of Pharmaceutical Sciences, University of Nottingham, Nottingham, NG7 2RD, UK

关键词: Subtilin;    Lantibiotics;    HPLC;    NMR;    Peptide conformation;    RP-HPLC;    reverse-phase high-pressure liquid chromatography;    2D NMR;    two-dimensional nuclear magnetic resonance;    HOHAHA;    homonuclear Hartmann—Hahn;    NOESY;    nuclear Overhauser enhancement spectroscopy;    FAB-MS;    fast atom bombardment mass spectroscopy;   

DOI  :  10.1016/0014-5793(92)80163-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Subtilin, a 32-amino acid peptide with potent antimicrobial activity, has been isolated from Bacillus subtilis ATCC6633. The chemical structure has been confirmed by the unambiguous sequence-specific assignment of its ¹H NMR spectrum. Detailed NMR analysis revealed that subtilin is a rather flexible molecule; the only observed conformational contraints were those imposed by the cyclic structures created by the tanthionine and 3-methyllanthionine residues. These results suggest that in aqueous solution subtilin and the homologous peptide nisin have similar conformation.

【 授权许可】

Unknown