Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata

Authors

  • Parthasarathy Sampathkumar,

    Corresponding author
    1. Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461
    2. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
    • Department of Biochemistry, Albert Einstein College of Medicine, Ullmann Building, Room 409, 1300 Morris Park Avenue, Bronx, NY 10461
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  • Seung Joong Kim,

    1. Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California 94158
    2. Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158
    3. California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158
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  • Danalyn Manglicmot,

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • Kevin T. Bain,

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • Jeremiah Gilmore,

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • Tarun Gheyi,

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • Jeremy Phillips,

    1. Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California 94158
    2. Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158
    3. California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158
    4. Graduate Group in Biological and Medical Informatics, University of California, San Francisco, California 94158
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  • Ursula Pieper,

    1. Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California 94158
    2. Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158
    3. California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158
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  • Javier Fernandez-Martinez,

    1. Laboratory of Cellular and Structural Biology, The Rockefeller University, New York 10065
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  • Josef D. Franke,

    1. Laboratory of Cellular and Structural Biology, The Rockefeller University, New York 10065
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  • Tsutomu Matsui,

    1. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California 94025
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  • Hiro Tsuruta,

    1. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California 94025
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  • Shane Atwell,

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • Devon A. Thompson,

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • J. Spencer Emtage,

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • Stephen R. Wasserman,

    1. LRL-CAT, Eli Lilly and Company, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois 60439
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  • Michael P. Rout,

    1. Laboratory of Cellular and Structural Biology, The Rockefeller University, New York 10065
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  • Andrej Sali,

    1. Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California 94158
    2. Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158
    3. California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158
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  • J. Michael Sauder,

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • Steven C. Almo,

    1. Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461
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  • Stephen K. Burley

    1. Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121
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  • Deceased on August 25, 2011

Abstract

The nuclear pore complex (NPC), embedded in the nuclear envelope, is a large, dynamic molecular assembly that facilitates exchange of macromolecules between the nucleus and the cytoplasm. The yeast NPC is an eightfold symmetric annular structure composed of ∼456 polypeptide chains contributed by ∼30 distinct proteins termed nucleoporins. Nup116, identified only in fungi, plays a central role in both protein import and mRNA export through the NPC. Nup116 is a modular protein with N-terminal “FG” repeats containing a Gle2p-binding sequence motif and a NPC targeting domain at its C-terminus. We report the crystal structure of the NPC targeting domain of Candida glabrata Nup116, consisting of residues 882–1034 [CgNup116(882–1034)], at 1.94 Å resolution. The X-ray structure of CgNup116(882–1034) is consistent with the molecular envelope determined in solution by small-angle X-ray scattering. Structural similarities of CgNup116(882–1034) with homologous domains from Saccharomyces cerevisiae Nup116, S. cerevisiae Nup145N, and human Nup98 are discussed. Proteins 2012; © 2012 Wiley Periodicals, Inc.

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