NMR assignment of backbone and side chain resonances for a dockerin-containing C-terminal fragment of the putative mu-toxin from Clostridium perfringens.
The mu-toxin of Clostridium perfringens, termed CpGH84A, is modular hydrolytic enzyme that contributes to the pathogenicity of this organism. Backbone and side chain 1H, 13C, and 15N resonance assignments have been determined for the C-terminal 15.5 kDa FIVAR-Doc modular pair of CpGH84A.
Chitayat
Seth
S
Department of Biochemistry, Queen's University, Kingston, ON, Canada.
Adams
Jarrett J
JJ
Smith
Steven P
SP
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001427:Bacterial Toxins / Q000737:chemistry* / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D003016:Clostridium perfringens / Q000737:chemistry* / Q000235:genetics / Q000472:pathogenicity; D017931:DNA Primers / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D001619:beta-N-Acetylhexosaminidases / Q000737:chemistry / Q000235:genetics
D001426:Bacterial Proteins; D001427:Bacterial Toxins; D017931:DNA Primers; D004269:DNA, Bacterial; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D006026:Glycoside Hydrolases; D001619:beta-N-Acetylhexosaminidases