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1H, 15N, and 13C backbone resonance assignments for the yersinia protein tyrosine phosphatase YopH

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Abstract

YopH is a protein tyrosine phosphatase that functions as a required virulence factor in Yersinia. Here we report the backbone resonance assignments for a point mutant of the C-terminal catalytic domain of YopH.

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Acknowledgments

We thank Jeff Hoch, Dmitry Korzhnev, Mark Maciejewski, Geoffrey Armstrong, and Marco Tonelli for access to, and assistance using, their high-field spectrometers. SKW and JPL acknowledge support from NIH grants T32GM008283 and NSF-MCB1121372.

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Authors and Affiliations

  1. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, USA

    Sean K. Whittier & J. Patrick Loria

  2. Department of Chemistry, Yale University, New Haven, CT, USA

    J. Patrick Loria

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  1. Sean K. Whittier
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  2. J. Patrick Loria
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Correspondence to J. Patrick Loria.

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Whittier, S.K., Loria, J.P. 1H, 15N, and 13C backbone resonance assignments for the yersinia protein tyrosine phosphatase YopH. Biomol NMR Assign 8, 387–389 (2014). https://doi.org/10.1007/s12104-013-9524-0

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  • DOI: https://doi.org/10.1007/s12104-013-9524-0

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