1H, 13C, and 15N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216᾿20) of a binary toxin from <em class=

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1H, 13C, and 15N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216᾿20) of a binary toxin from

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作者：Braden M. Roth ; Raquel Godoy-Ruiz ; Kristen M. Varney…
关键词：Clostridium difficile ; CDI ; CDTa ; Binary toxin ; ADP ; ribosyltransferase
刊名：Biomolecular NMR Assignments
出版年：2016
出版时间：April 2016
年：2016
卷：10
期：1
页码：213-217
全文大小：1,420 KB
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Gülke I, Pfeifer G, Liese J et al (2001) Characterization of the enzymatic component of the ADP-ribosyltransferase toxin CDTa from Clostridium difficile. Infect Immun 69:6004–6011. doi:10.1128/IAI.69.10.6004-6011.2001 CrossRef
Papatheodorou P, Carette JE, Bell GW et al (2011) Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT). Proc Natl Acad Sci USA 108:16422–16427. doi:10.1073/pnas.1109772108 ADS CrossRef
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作者单位：Braden M. Roth (1)
Raquel Godoy-Ruiz (1)
Kristen M. Varney (1)
Richard R. Rustandi (2)
David J. Weber (1)

1. Center for Biomolecular Therapeutics (CBT), Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD, 21201, USA
2. Department of Vaccine Analytical Development, Merck Research Laboratories, 770 Sumneytown Pike, West Point, PA, 19486, USA
刊物类别：Physics and Astronomy
刊物主题：None Assigned
出版者：Springer Netherlands
ISSN：1874-270X

文摘

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; 1–215CDTa) that interacts with CDTb and a C-terminal domain (residues 216–420; 216–420CDTa) that harbors the intact ADP-ribosyltransferase (ART) active site. Reported here are the 1H, 13C, and 15N backbone resonance assignments of the 23 kDa, 205 amino acid C-terminal enzymatic domain of CDTa, termed 216–420CDTa. These NMR resonance assignments for 216–420CDTa 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.