TY - JOUR
T1 - Complete covalent structure of nisin Q, new natural nisin variant, containing post-translationally modified amino acids
AU - Fukao, Masanori
AU - Obita, Takayuki
AU - Yoneyama, Fuminori
AU - Kohda, Daisuke
AU - Zendo, Takeshi
AU - Nakayama, Jiro
AU - Sonomoto, Kenji
N1 - Funding Information:
This work was supported in part by the Regional Industry Revitalization Project of the Ministry of Economy, Trade, and Industry of Japan, and by Grants-in-Aid for Scientific Research from the Japan Society for the Promotion of Science (JSPS).
PY - 2008
Y1 - 2008
N2 - The third member of the nisin variant, nisin Q, produced by Lactococcus lactis 61-14, is a ribosomally-synthesized antimicrobial peptide, the so-called lantibiotic containing post-translationally modified amino acids such as lanthionine and dehydroalanine. Here, we determined the complete covalent structure of nisin Q, consisting of 34 amino acids, by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy. Sequential assignment of nisin Q containing the unusual amino acids was performed by total correlation spectroscopy (TOCSY) and nuclear Overhauser enhancement spectroscopy (NOESY). The observed long range nuclear Overhauser effect (NOE) in nisin Q indicated assignment of all five sets of lanthionines that intramolecularly bridge residues 3-7, 8-11, 13-19, 23-26, and 25-28. Consequently, the covalent structure of nisin Q was determined to hold the same thioether linkage formation as the other two nisins, but to harbor the four amino acid substitutions, in contrast with nisin A.
AB - The third member of the nisin variant, nisin Q, produced by Lactococcus lactis 61-14, is a ribosomally-synthesized antimicrobial peptide, the so-called lantibiotic containing post-translationally modified amino acids such as lanthionine and dehydroalanine. Here, we determined the complete covalent structure of nisin Q, consisting of 34 amino acids, by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy. Sequential assignment of nisin Q containing the unusual amino acids was performed by total correlation spectroscopy (TOCSY) and nuclear Overhauser enhancement spectroscopy (NOESY). The observed long range nuclear Overhauser effect (NOE) in nisin Q indicated assignment of all five sets of lanthionines that intramolecularly bridge residues 3-7, 8-11, 13-19, 23-26, and 25-28. Consequently, the covalent structure of nisin Q was determined to hold the same thioether linkage formation as the other two nisins, but to harbor the four amino acid substitutions, in contrast with nisin A.
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U2 - 10.1271/bbb.80066
DO - 10.1271/bbb.80066
M3 - Article
C2 - 18603791
AN - SCOPUS:47949121069
SN - 0916-8451
VL - 72
SP - 1750
EP - 1755
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 7
ER -