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NMR assignment of backbone and side chain resonances for a dockerin-containing C-terminal fragment of the putative μ-toxin from Clostridium perfringens

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Abstract

The μ-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.

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Acknowledgements

We acknowledge Dr. Tara Sprules for data collection on the 800 MHz spectrometer and technical support at the Québec/Eastern Canada High Field NMR Facility. This work was supported by a CIHR operating grant to S.P.S. (MOP-77776). S.C. is the recipient of a Franklin Bracken doctoral scholarship. J.J.A. is supported by a NSERC doctoral award. S.P.S. is a Canadian Institutes of Health Research New Investigator.

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Authors and Affiliations

  1. Department of Biochemistry, Queen’s University, Kingston, ON, Canada, K7L 3N6

    Seth Chitayat, Jarrett J. Adams & Steven P. Smith

  2. Protein Function Discovery Group, Queen’s University, Kingston, ON, Canada, K7L 3N6

    Steven P. Smith

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  1. Seth Chitayat
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  2. Jarrett J. Adams
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  3. Steven P. Smith
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Correspondence to Steven P. Smith.

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Chitayat, S., Adams, J.J. & Smith, S.P. NMR assignment of backbone and side chain resonances for a dockerin-containing C-terminal fragment of the putative μ-toxin from Clostridium perfringens . Biomol NMR Assign 1, 13–15 (2007). https://doi.org/10.1007/s12104-007-9002-7

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  • DOI: https://doi.org/10.1007/s12104-007-9002-7

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