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1H, 13C and 15N resonance assignments and peptide binding site chemical shift perturbation mapping for the Escherichia coli redox enzyme chaperone DmsD

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Abstract

Herein are reported the mainchain 1H, 13C and 15N chemical shift assignments and amide 15N relaxation data for Escherichia coli DmsD, a 23.3 kDa protein responsible for the correct folding and translocation of the dimethyl sulfoxide reductase enzyme complex. In addition, the observed amide chemical shift perturbations resulting from complex formation with the reductase subunit DmsA leader peptide support a model in which the 44 residue peptide makes extensive contacts across the surface of the DmsD protein.

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Acknowledgments

The authors would like to acknowledge Eric Escobar, Hyun-Seo Kang and Kelly Kim for assistance with Sparky and assignment techniques and Dr. R. J. Turner for providing the plasmid from which our DmsD construct was cloned. NMR instrument support was provided by the Canadian Institutes for Health Research (CIHR), the Canadian Foundation for Innovation (CFI), the British Columbia Knowledge Development Fund (BCKDF), the UBC Blusson Fund, and the Michael Smith Foundation for Health Research (MSFHR). M. P. acknowledges funding from the National Science and Engineering Research Council of Canada (NSERC), CIHR and MSFHR. L. M. acknowledges funding from NSERC.

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Authors and Affiliations

  1. Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC, V5A 1S6, Canada

    Charles M. Stevens & Mark Paetzel

  2. Department of Biochemistry and Molecular Biology, Department of Chemistry, and the Michael Smith Laboratories, The University of British Columbia, Life Sciences Centre, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada

    Mark Okon & Lawrence P. McIntosh

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  1. Charles M. Stevens
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  2. Mark Okon
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  3. Lawrence P. McIntosh
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  4. Mark Paetzel
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Correspondence to Lawrence P. McIntosh or Mark Paetzel.

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Stevens, C.M., Okon, M., McIntosh, L.P. et al. 1H, 13C and 15N resonance assignments and peptide binding site chemical shift perturbation mapping for the Escherichia coli redox enzyme chaperone DmsD. Biomol NMR Assign 7, 193–197 (2013). https://doi.org/10.1007/s12104-012-9408-8

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  • DOI: https://doi.org/10.1007/s12104-012-9408-8

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