Complete covalent structure of nisin Q, new natural nisin variant, containing post-translationally modified amino acids
Complete covalent structure of nisin Q, new natural nisin variant, containing post-translationally modified amino acids
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DOI:
10.1271/bbb.80066
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发表时间:
2008-07-01
影响因子:
1.6
通讯作者:
Sonomoto, Kenji
中科院分区:
文献类型:
--
作者:
Fukao, Masanori;Obita, Takayuki;Sonomoto, Kenji
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 H-1 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.