Format

Send to

Choose Destination
See comment in PubMed Commons below
Biosci Biotechnol Biochem. 2008 Jul;72(7):1750-5. Epub 2008 Jul 7.

Complete covalent structure of nisin Q, new natural nisin variant, containing post-translationally modified amino acids.

Author information

1
Department of Bioscience and Biotechnology, Division of Microbial Science and Technology, Faculty of Agriculture, Laboratory of Microbial Technology, Graduate School, Kyushu University, Fukuoka, Japan.

Abstract

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 (1)H 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.

PMID:
18603791
DOI:
10.1271/bbb.80066
[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Taylor & Francis Icon for J-STAGE, Japan Science and Technology Information Aggregator, Electronic
    Loading ...
    Support Center