3pbp | pdb_00003pbp

Structure of the yeast heterotrimeric Nup82-Nup159-Nup116 nucleoporin complex

spinqualitylabelsall models 3pbp, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pbp is a 12 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PGE NonStd Res: MSE Gene: NUP82, YJL061W, J1135, HRB187 (Saccharomyces cerevisiae), NUP116, NSP116, YMR047C, YM9532.12C (Saccharomyces cerevisiae), NUP159, NUP158, RAT7, YIL115C (Saccharomyces cerevisiae) Resources: FirstGlance, OCA, RCSB, PDBsum Function [NU159_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export. [NU116_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP116 plays an important role in several nuclear export and import pathways including poly(A)+ RNA, tRNA, pre-ribosome, and protein transport. Publication Abstract from PubMed So far, only a few of the interactions between the approximately 30 nucleoporins comprising the modular structure of the nuclear pore complex have been defined at atomic resolution. Here we report the crystal structure, at 2.6 A resolution, of a heterotrimeric complex, composed of fragments of three cytoplasmically oriented nucleoporins of yeast: Nup82, Nup116, and Nup159. Our data show that the Nup82 fragment, representing more than the N-terminal half of the molecule, folds into an extensively decorated, seven-bladed beta-propeller that forms the centerpiece of this heterotrimeric complex and anchors both a C-terminal fragment of Nup116 and the C-terminal tail of Nup159. Binding between Nup116 and Nup82 is mutually reinforced via two loops, one emanating from the Nup82 beta-propeller and the other one from the beta-sandwich fold of Nup116, each contacting binding pockets in their counterparts. The Nup82-Nup159 interaction occurs through an amphipathic alpha-helix of Nup159, which is cradled in a large hydrophobic groove that is generated from several large surface decorations of the Nup82 beta-propeller. Although Nup159 and Nup116 fragments bind to the Nup82 beta-propeller in close vicinity, there are no direct contacts between them, consistent with the noncooperative binding that was detected biochemically. Extensive mutagenesis delineated hot-spot residues for these interactions. We also showed that the Nup82 beta-propeller binds to other yeast Nup116 family members, Nup145N, Nup100 and to the mammalian homolog, Nup98. Notably, each of the three nucleoporins contains additional nuclear pore complex binding sites, distinct from those that were defined here in the heterotrimeric Nup82*Nup159*Nup116 complex. Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex.,Yoshida K, Seo HS, Debler EW, Blobel G, Hoelz A Proc Natl Acad Sci U S A. 2011 Oct 4;108(40):16571-6. Epub 2011 Sep 19. PMID:21930948 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nucleoporin

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