title: Structural basis of the nic96 subcomplex organization in the nuclear pore channel.
abstract: Nic96 is a conserved nucleoporin that recruits the Nsp1-Nup49-Nup57 complex, a module with Phe-Gly (FG) repeats, to the central transport channel of the nuclear pore complex (NPC). Nic96 binds the Nsp1 complex via its N domain and assembles into the NPC framework via its central and C domain. Here, we report the crystal structure of a large structural nucleoporin, Nic96 without its N domain (Nic96DeltaN). Nic96DeltaN is composed of three domains and is a straight molecule that--although almost entirely helical--exhibits strong deviations from the predicted alpha-solenoid fold. The missing N domain projects midway from the Nic96 molecule, indicating how the Nsp1 complex might be located with respect to the rod-like Nic96. Notably, Nic96DeltaN binds in vitro to FG repeats of the Nsp1 complex. These data suggest a model of how Nic96 could organize a transport module with coiled-coil domains and FG repeats in the central pore channel.
authors.affiliation: Max-Planck-Institut für Molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
authors.forename: Nils
authors.initials: N
authors.lastname: Schrader
authors.forename: Philipp
authors.initials: P
authors.lastname: Stelter
authors.forename: Dirk
authors.initials: D
authors.lastname: Flemming
authors.forename: Ruth
authors.initials: R
authors.lastname: Kunze
authors.forename: Ed
authors.initials: E
authors.lastname: Hurt
authors.forename: Ingrid R
authors.initials: IR
authors.lastname: Vetter
mesh_terms: D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000648:ultrastructure; D018360:Crystallography, X-Ray; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D008854:Microscopy, Electron; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D022022:Nuclear Pore / Q000737:chemistry* / Q000648:ultrastructure; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry* / Q000648:ultrastructure; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D017354:Point Mutation; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D020449:Repetitive Sequences, Amino Acid; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D013329:Structure-Activity Relationship
chemical_list: D002135:Calcium-Binding Proteins; D008565:Membrane Proteins; D046912:Multiprotein Complexes; C082533:NIC96 protein, S cerevisiae; C062748:NSP1 protein, S cerevisiae; C077727:NUP49 protein, S cerevisiae; C091559:NUP57 protein, S cerevisiae; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins