NDLI: $^{1}$H, $^{13}$C, and $^{15}$N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216–420) of a binary toxin from Clostridium difficile

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$^{1}$H, $^{13}$C, and $^{15}$N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216–420) of a binary toxin from Clostridium difficile

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$^{1}$H, $^{13}$C, and $^{15}$N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216–420) of a binary toxin from Clostridium difficile

Content Provider	Springer Nature Link
Author	Roth, Braden M. Godoy Ruiz, Raquel Varney, Kristen M. Rustandi, Richard R. Weber, David J.
Copyright Year	2016
Abstract	Clostridium difficile is a bacterial pathogen and is the most commonly reported source of nosocomial infection in industrialized nations. Symptoms of C. difficile infection (CDI) include antibiotic-associated diarrhea, pseudomembranous colitis, sepsis and death. Over the last decade, rates and severity of hospital infections in North America and Europe have increased dramatically and correlate with the emergence of a hypervirulent strain of C. difficile characterized by the presence of a binary toxin, CDT (C. difficile toxin). The binary toxin consists of an enzymatic component (CDTa) and a cellular binding component (CDTb) that together form the active binary toxin complex. CDTa harbors a pair of structurally similar but functionally distinct domains, an N-terminal domain (residues 1–215; $^{1–215}$CDTa) that interacts with CDTb and a C-terminal domain (residues 216–420; $^{216–420}$CDTa) that harbors the intact ADP-ribosyltransferase (ART) active site. Reported here are the $^{1}$H, $^{13}$C, and $^{15}$N backbone resonance assignments of the 23 kDa, 205 amino acid C-terminal enzymatic domain of CDTa, termed $^{216–420}$CDTa. These NMR resonance assignments for $^{216–420}$CDTa represent the first for a family of ART binary toxins and provide the framework for detailed characterization of the solution-state protein structure determination, dynamic studies of this domain, as well as NMR-based drug discovery efforts.
Starting Page	213
Ending Page	217
Page Count	5
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	10
Issue Number	1
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-02-17
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Clostridium difficile CDI CDTa Binary toxin ADP-ribosyltransferase Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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Detection of the ADP-ribosyltransferase toxin gene (cdtA) and its activity in Clostridium difficile isolates from Equidae.

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$^{1}$H, $^{13}$C, and $^{15}$N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216–420) of a binary toxin from Clostridium difficile

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