Structure and function of Escherichia coli RimK, an ATP-grasp fold, l-glutamyl ligase enzyme

Authors

  • Gengxiang Zhao,

    1. Department of Integrative Systems Biology, Center for Genetic Medicine Research, Children's National Medical Center, The George Washington University, Washington, DC
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  • Zhongmin Jin,

    1. Southeast Regional Collaborative Access Team, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois
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  • Yanli Wang,

    1. National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland
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  • Norma M. Allewell,

    1. Department of Cell Biology and Molecular Genetics, College of Computer, Mathematical, and Natural Sciences, University of Maryland, College Park, Maryland
    2. Department of Chemistry and Biochemistry, College of Computer, Mathematical, and Natural Sciences, University of Maryland, College Park, Maryland
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  • Mendel Tuchman,

    1. Department of Integrative Systems Biology, Center for Genetic Medicine Research, Children's National Medical Center, The George Washington University, Washington, DC
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  • Dashuang Shi

    Corresponding author
    1. Department of Integrative Systems Biology, Center for Genetic Medicine Research, Children's National Medical Center, The George Washington University, Washington, DC
    2. Key Laboratory of Organo-Pharmaceutical Chemistry, Jiangxi Province, Gannan Normal University, Ganzhou, People's Republic of China
    • Correspondence to: Dashuang Shi, Department of Integrative Systems Biology, Center for Genetic Medicine Research, Children's National Medical Center, The George Washington University, 111 Michigan Avenue, N.W., Washington, DC 20010-2970. E-mail: dshi@cnmcresearch.org

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ABSTRACT

We report herein the crystal structure of Escherichia coli RimK at a resolution of 2.85 Å, an enzyme that catalyzes the post-translational addition of up to 15 C-terminal glutamate residues to ribosomal protein S6. The structure belongs to the ATP-grasp superfamily and is organized as a tetramer, consistent with gel filtration analysis. Each subunit consists of three distinct structural domains and the active site is located in the cleft between these domains. The catalytic reaction appears to occur at the junction between the three domains as ATP binds between the B and C domains, and other substrates bind nearby.Proteins 2013; 81:1847–1854. © 2013 Wiley Periodicals, Inc.

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