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 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 1 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

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Keywords

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

Cite this

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. / 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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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, S 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

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.

In: Proteins: Structure, Function and Bioinformatics, Vol. 80, No. 8, 01.08.2012, p. 2110-2116.

Research output: Contribution to journalArticle

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T1 - Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata

AU - Sampathkumar, Parthasarathy

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

PY - 2012/8/1

Y1 - 2012/8/1

N2 - 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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KW - MRNA export

KW - Nuclear pore complex

KW - Nup100

KW - Nup116

KW - Nup145

KW - Nup98

KW - Structural genomics

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