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

作者：Sampathkumar Parthasarathy^*; Kim Seung Joong; Manglicmot D****yn; 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

来源：Proteins: Structure, Function, and Genetics , 2012, 80(8): 2110-2116.

DOI：10.1002/prot.24102

• nuclear pore complex
• Nup116
• Nup98
• Nup100
• Nup145
• mRNA export
• 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 the cytoplasm. The yeast NPC is an eightfold symmetric annular structure composed of similar to 456 polypeptide chains contributed by similar to 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 8821034 [CgNup116(8821034)], at 1.94 angstrom resolution. The X-ray structure of CgNup116(8821034) is consistent with the molecular envelope determined in solution by small-angle X-ray scattering. Structural similarities of CgNup116(8821034) with homologous domains from Saccharomyces cerevisiae Nup116, S. cerevisiae Nup145N, and human Nup98 are discussed.

• 出版日期2012-8