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

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...

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Veröffentlicht in:	FEBS letters 1992-03, Vol.300 (1), p.56-62
Hauptverfasser:	Chan, Weng C., Bycroft, Barrie W., Leyland, Mark L., Lian, Lu-Yun, Yang, J.C., Roberts, Gordon C.K.
Format:	Artikel
Sprache:	eng
Schlagworte:	2D NMR Amino Acid Sequence Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Anti-Bacterial Agents - chemistry Anti-Bacterial Agents - isolation & purification Anti-Bacterial Agents - metabolism Bacillus subtilis Bacterial Proteins Bacteriocins Biochemistry & Molecular Biology Biological and medical sciences Biophysics Cell Biology Chromatography, High Pressure Liquid conformation FAB-MS fast atom bombardment mass spectroscopy Fundamental and applied biological sciences. Psychology HOHAHA homonuclear Hartmann—Hahn HPLC Lantibiotics Life Sciences & Biomedicine Magnetic Resonance Spectroscopy Molecular Sequence Data Molecular Structure N.M.R NMR NOESY nuclear Overhauser enhancement spectroscopy Peptide conformation Peptides Peptides, Cyclic - chemistry Peptides, Cyclic - isolation & purification Peptides, Cyclic - metabolism Protein Conformation Proteins reverse-phase high-pressure liquid chromatography RP-HPLC Science & Technology Solutions Structure-Activity Relationship Subtilin two-dimensional nuclear magnetic resonance
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Beschreibung
Zusammenfassung:	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.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(92)80163-B