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 molecule; the only observed conformational contraints were those imposed by the cyclic structures created by the lanthionine and 3-methyllanthionine residues. These results suggest that in aqueous solution subtilin and the homologous peptide nisin have similar conformations.
Chan
W C
WC
Department of Pharmaceutical Sciences, University of Nottingham, UK.
Bycroft
B W
BW
Leyland
M L
ML
Lian
L Y
LY
Yang
J C
JC
Roberts
G C
GC
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D001426:Bacterial Proteins; D001430:Bacteriocins; D002851:Chromatography, High Pressure Liquid; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides; D010456:Peptides, Cyclic / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D012996:Solutions; D013329:Structure-Activity Relationship
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D001430:Bacteriocins; D010455:Peptides; D010456:Peptides, Cyclic; D012996:Solutions; C002836:subtilin