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; Stephen K Burley; Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

doi:10.1002/prot.24102

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Atomic Structure of the Nuclear Pore Complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata

Journal article

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Peer reviewed

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, …

Proteins, structure, function, and bioinformatics, Vol.80(8), pp.2110-2116

08/2012

DOI: https://doi.org/10.1002/prot.24102

PMCID: PMC3686472

PMID: 22544723

Abstract

mRNA export

Nuclear Pore Complex

Nup100

Nup116

Nup145

Nup98

structural genomics

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 cytoplasm. The yeast NPC is an eight-fold symmetric annular structure composed of ~456 polypeptide chains contributed by ~30 distinct proteins termed nucleoporins (Nups). 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 (GLEBS 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 (SAXS). 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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Title: Atomic Structure of the Nuclear Pore Complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata
Creators: Parthasarathy Sampathkumar - Department of Biochemistry, Ullmann Building, Room 409, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461
Seung Joong Kim - Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94158
Danalyn Manglicmot - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
Kevin T Bain - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
Jeremiah Gilmore - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
Tarun Gheyi - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
Jeremy Phillips - Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94158
Ursula Pieper - Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94158
Javier Fernandez-Martinez - Laboratory of Cellular and Structural Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA
Josef D Franke - Laboratory of Cellular and Structural Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA
Tsutomu Matsui - Stanford Synchrotron Radiation Lightsource, Stanford Linear Accelerator Center, 2575 Sand Hill Road, MS 69, Menlo Park, CA 94025-7015, USA
Hiro Tsuruta - Stanford Synchrotron Radiation Lightsource, Stanford Linear Accelerator Center, 2575 Sand Hill Road, MS 69, Menlo Park, CA 94025-7015, USA
Shane Atwell - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
Devon A Thompson - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
J. Spencer Emtage - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
Stephen R Wasserman - LRL-CAT, Eli Lilly and Company, Advanced Photon Source, Argonne National Laboratory, Building 401, 9700 South Cass Avenue, Argonne, IL 60439 USA
Michael P Rout - Laboratory of Cellular and Structural Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA
Andrej Sali - Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA 94158
J. Michael Sauder - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
Steven C Almo - Department of Biochemistry, Ullmann Building, Room 409, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461
Stephen K Burley - Translational Sciences and Technology (TS&T), Eli Lilly and Company, Lilly Biotechnology Center, 10300 Campus Point Drive, Suite 200, San Diego, CA 92121, USA
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Publication Details: Proteins, structure, function, and bioinformatics, Vol.80(8), pp.2110-2116
Date published: 08/2012
Grant note: U01 GM098256 || GM / National Institute of General Medical Sciences : NIGMS R01 GM083960 || GM / National Institute of General Medical Sciences : NIGMS R01 GM062427 || GM / National Institute of General Medical Sciences : NIGMS U54 RR022220 || RR / National Center for Research Resources : NCRR U54 GM094662 || GM / National Institute of General Medical Sciences : NIGMS
Academic Unit: Chemistry and Chemical Biology (SAS); Institute for Quantitative Biomedicine
Language: English
Resource Type: Journal article
Identifiers: 991031665917304646