Sequence-specific 1H, 15N and 13C resonance assignments of the 23.7-kDa homodimeric toxin CcdB from Vibrio fischeri.

TitleSequence-specific 1H, 15N and 13C resonance assignments of the 23.7-kDa homodimeric toxin CcdB from Vibrio fischeri.
Publication TypeJournal Article
Year of Publication2009
AuthorsRespondek, M., L. Buts, N. De Jonge, S. Haesaerts, R. Loris, L. Van Melderen, L. Wyns, and K. Zangger
JournalBiomol NMR Assign
Volume3
Issue1
Pagination145-7
Date Published2009 Jun
ISSN1874-270X
KeywordsAliivibrio fischeri, Amino Acid Sequence, Bacterial Proteins, Bacterial Toxins, Carbon Isotopes, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Molecular Weight, Nitrogen Isotopes, Protein Structure, Tertiary, Protein Subunits, Protons
Abstract

CcdB is the toxic component of a bacterial toxin-antitoxin system. It inhibits DNA gyrase (a type II topoisomerase), and its toxicity can be neutralized by binding of its antitoxin CcdA. Here we report the sequential backbone and sidechain (1)H, (15)N and (13)C resonance assignments of CcdB(Vfi) from the marine bacterium Vibrio fischeri. The BMRB accession number is 16135.

DOI10.1007/s12104-009-9161-9
Alternate JournalBiomol NMR Assign
PubMed ID19636967