Structure Note

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

  1. Parthasarathy Sampathkumar1,2,*,
  2. Seung Joong Kim3,4,5,
  3. Danalyn Manglicmot2,
  4. Kevin T. Bain2,
  5. Jeremiah Gilmore2,
  6. Tarun Gheyi2,
  7. Jeremy Phillips3,4,5,6,
  8. Ursula Pieper3,4,5,
  9. Javier Fernandez-Martinez7,
  10. Josef D. Franke7,
  11. Tsutomu Matsui8,
  12. Hiro Tsuruta8,
  13. Shane Atwell2,
  14. Devon A. Thompson2,
  15. J. Spencer Emtage2,
  16. Stephen R. Wasserman9,
  17. Michael P. Rout7,
  18. Andrej Sali3,4,5,
  19. J. Michael Sauder2,
  20. Steven C. Almo1,
  21. Stephen K. Burley2

Article first published online: 4 JUN 2012

DOI: 10.1002/prot.24102

Issue

Proteins: Structure, Function, and Bioinformatics

Proteins: Structure, Function, and Bioinformatics

Volume 80, Issue 8, pages 2110–2116, August 2012

Additional Information

How to Cite

Sampathkumar, P., Kim, S. J., Manglicmot, D., Bain, K. T., Gilmore, J., Gheyi, T., Phillips, J., Pieper, U., Fernandez-Martinez, J., Franke, J. D., Matsui, T., Tsuruta, H., Atwell, S., Thompson, D. A., Emtage, J. S., Wasserman, S. R., Rout, M. P., Sali, A., Sauder, J. M., Almo, S. C. and Burley, S. K. (2012), Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata. Proteins, 80: 2110–2116. doi: 10.1002/prot.24102

Author Information

  1. 1

    Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461

  2. 2

    Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121

  3. 3

    Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California 94158

  4. 4

    Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158

  5. 5

    California Institute for Quantitative Biosciences, University of California, San Francisco, California 94158

  6. 6

    Graduate Group in Biological and Medical Informatics, University of California, San Francisco, California 94158

  7. 7

    Laboratory of Cellular and Structural Biology, The Rockefeller University, New York 10065

  8. 8

    Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, California 94025

  9. 9

    LRL-CAT, Eli Lilly and Company, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois 60439

*Department of Biochemistry, Albert Einstein College of Medicine, Ullmann Building, Room 409, 1300 Morris Park Avenue, Bronx, NY 10461

  1. †

    Deceased on August 25, 2011

Publication History

  1. Issue published online: 7 JUL 2012
  2. Article first published online: 4 JUN 2012
  3. Accepted manuscript online: 27 APR 2012 08:53AM EST
  4. Manuscript Accepted: 11 APR 2012
  5. Manuscript Revised: 5 APR 2012
  6. Manuscript Received: 27 JAN 2012

Funded by

  • NIH. Grant Numbers: U54 GM074945, U54 GM094662
  • NIH. Grant Number: R01 GM062427 (MPR)
  • NIH. Grant Number: R01 GM083960
  • NIH. Grant Number: U54 RR022220
  • The US Department of Energy, Office of Basic Energy Sciences
  • the DOE Office of Biological and Environmental Research
  • The National Institutes of Health, National Center for Research Resources, Biomedical Technology Program. Grant Number: P41RR001209

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Keywords:

  • nuclear pore complex;
  • Nup116;
  • Nup98;
  • Nup100;
  • Nup145;
  • mRNA export;
  • structural genomics

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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