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. Almo & 1 others Stephen K. Burley

Research output: Contribution to journalArticle

6 Citations (Scopus)

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
StatePublished - Aug 2012

Fingerprint

Candida glabrata
Nuclear Pore
Candida
Yeast
Yeasts
Nuclear Pore Complex Proteins
Proteins
Saccharomyces cerevisiae
Fungi
X ray scattering
Macromolecules
X-Rays
Molecular dynamics
Crystal structure
Terminal Repeat Sequences
Nuclear Envelope
X rays
Molecular Dynamics Simulation
Messenger RNA
Peptides

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Cite this

Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata. / Sampathkumar, Parthasarathy; Kim, Seung Joong; Manglicmot, Danalyn; Bain, Kevin T.; Gilmore, Jeremiah; Gheyi, Tarun; Phillips, Jeremy; Pieper, Ursula; Fernandez-Martinez, Javier; Franke, Josef D.; Matsui, Tsutomu; Tsuruta, Hiro; Atwell, Shane; Thompson, Devon A.; Emtage, J. Spencer; Wasserman, Stephen R.; Rout, Michael P.; Sali, Andrej; Sauder, J. Michael; Almo, Steven C.; Burley, Stephen K.

In: Proteins: Structure, Function and Bioinformatics, Vol. 80, No. 8, 08.2012, p. 2110-2116.

Research output: Contribution to journalArticle

Sampathkumar, P, Kim, SJ, Manglicmot, D, Bain, KT, Gilmore, J, Gheyi, T, Phillips, J, Pieper, U, Fernandez-Martinez, J, Franke, JD, Matsui, T, Tsuruta, H, Atwell, S, Thompson, DA, Emtage, JS, Wasserman, SR, Rout, MP, Sali, A, Sauder, JM, Almo, SC & Burley, SK 2012, 'Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata', Proteins: Structure, Function and Bioinformatics, vol. 80, no. 8, pp. 2110-2116. https://doi.org/10.1002/prot.24102
Sampathkumar, Parthasarathy ; Kim, Seung Joong ; Manglicmot, Danalyn ; Bain, Kevin T. ; Gilmore, Jeremiah ; Gheyi, Tarun ; Phillips, Jeremy ; Pieper, Ursula ; Fernandez-Martinez, Javier ; Franke, Josef D. ; Matsui, Tsutomu ; Tsuruta, Hiro ; Atwell, Shane ; Thompson, Devon A. ; Emtage, J. Spencer ; Wasserman, Stephen R. ; Rout, Michael P. ; Sali, Andrej ; Sauder, J. Michael ; Almo, Steven C. ; Burley, Stephen K. / Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata. In: Proteins: Structure, Function and Bioinformatics. 2012 ; Vol. 80, No. 8. pp. 2110-2116.
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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 {\AA} 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.",
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AU - Kim, Seung Joong

AU - Manglicmot, Danalyn

AU - Bain, Kevin T.

AU - Gilmore, Jeremiah

AU - Gheyi, Tarun

AU - Phillips, Jeremy

AU - Pieper, Ursula

AU - Fernandez-Martinez, Javier

AU - Franke, Josef D.

AU - Matsui, Tsutomu

AU - Tsuruta, Hiro

AU - Atwell, Shane

AU - Thompson, Devon A.

AU - Emtage, J. Spencer

AU - Wasserman, Stephen R.

AU - Rout, Michael P.

AU - Sali, Andrej

AU - Sauder, J. Michael

AU - Almo, Steven C.

AU - Burley, Stephen K.

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AB - 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.

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