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3NF5

Crystal structure of the C-terminal domain of nuclear pore complex component NUP116 from Candida glabrata

Summary for 3NF5
Entry DOI10.2210/pdb3nf5/pdb
DescriptorNucleoporin NUP116, GLYCEROL (3 entities in total)
Functional Keywordsnuclear pore complex, nup116, glebs domain, structural genomics, psi-2, protein structure initiative, new york structural genomix research consortium, nysgxrc, new york sgx research center for structural genomics, protein transport
Biological sourceCandida glabrata (yeast)
Total number of polymer chains2
Total formula weight38080.00
Authors
Primary citationSampathkumar, 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.,Burley, S.K.
Atomic structure of the nuclear pore complex targeting domain of a Nup116 homologue from the yeast, Candida glabrata.
Proteins, 80:2110-2116, 2012
Cited by
PubMed 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.
PubMed: 22544723
DOI: 10.1002/prot.24102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.94 Å)
Structure validation

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數據於2025-07-23公開中

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