Crystal structure of Methanobacterium thermoautotrophicum conserved protein MTH1020 reveals an NTN-hydrolase fold

Authors

  • Vivian Saridakis,

    1. Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Ontario, Canada
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  • Dinesh Christendat,

    Corresponding author
    1. Clinical Genomics Center, University Health Network, Toronto, Ontario, Canada
    • Dinesh Christendar, Clinical Genomics Center, University Health Network, 101 College Street, Toronto, Ontario, M5G 1L7, Canada
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  • Anders Thygesen,

    1. Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Ontario, Canada
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  • Cheryl H. Arrowsmith,

    1. Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Ontario, Canada
    2. Clinical Genomics Center, University Health Network, Toronto, Ontario, Canada
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  • Aled M. Edwards,

    1. Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Ontario, Canada
    2. Clinical Genomics Center, University Health Network, Toronto, Ontario, Canada
    3. Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada
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  • Emil F. Pai

    1. Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Ontario, Canada
    2. Departments of Medical Biophysics, Biochemistry and Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, Canada
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  • The atomic coordinates for MTH1020 (code 1KUU) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org).

  • Use of the Advanced Photon Source was supported by the Basic Energy Sciences, Office of Science, United States Department of Energy, under Contract W-31-109-Eng-38. Use of the BioCARS Sector 14 was supported by the National Center for Research Resources, National Institutes of Health, under Grant RR07707.

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