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

Parthasarathy Sampathkumar, Seung Joong Kim, Danalyn Manglicmot, Kevin T. Bain, Jeremiah Gilmore, Tarun Gheyi, Jeremy Phillips, Ursula Pieper, Javier Fernandez-Martinez, Josef D. Franke, Tsutomu Matsui, Hiro Tsuruta, Shane Atwell, Devon A. Thompson, J. Spencer Emtage, Stephen R. Wasserman, Michael P. Rout, Andrej Sali, J. Michael Sauder, Steven C. AlmoStephen K. Burley

Research output: Contribution to journalArticle

6 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)2110-2116
Number of pages7
JournalProteins: Structure, Function and Bioinformatics
Volume80
Issue number8
DOIs
Publication statusPublished - Aug 1 2012

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Keywords

  • MRNA export
  • Nuclear pore complex
  • Nup100
  • Nup116
  • Nup145
  • Nup98
  • Structural genomics

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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