Proteopedia

2qx5

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Structure of nucleoporin Nic96Structure of nucleoporin Nic96

Structural highlights

2qx5 is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:NIC96 (ATCC 18824)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NIC96_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. NIC96, which is localized to the core of the NPC and the distal ring of the nuclear basket, is required for de novo assembly of NPCs. It is involved in nuclear GSP1 import.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The nuclear pore complex (NPC) is an elaborate protein machine that mediates macromolecular transport across the nuclear envelope in all eukaryotes. The NPC is formed by nucleoporins that assemble in multiple copies around an 8-fold symmetry axis. Homology modeling suggests that most architectural nucleoporins are composed of simple beta-propeller and alpha-helical repeat domains. Here we present the crystal structure of Nic96, the Nup93 homolog in Saccharomyces cerevisiae, one of the major components of the NPC. This is the first structure of an alpha-helical nucleoporin domain. The protein folds into an elongated, mostly alpha-helical structure. Characteristically, non-canonical architectural features define the Nic96 structure. Sequence conservation among Nup93 homologs across all eukaryotes strongly suggests that the distinct topology is evolutionarily well maintained. We propose that the unique Nic96/Nup93 fold has a conserved function in all eukaryotes.

Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture.,Jeudy S, Schwartz TU J Biol Chem. 2007 Nov 30;282(48):34904-12. Epub 2007 Sep 25. PMID:17897938[12]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Grandi P, Schlaich N, Tekotte H, Hurt EC. Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p. EMBO J. 1995 Jan 3;14(1):76-87. PMID:7828598
  2. ↑ Nehrbass U, Rout MP, Maguire S, Blobel G, Wozniak RW. The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex. J Cell Biol. 1996 Jun;133(6):1153-62. PMID:8682855
  3. ↑ Schlaich NL, Haner M, Lustig A, Aebi U, Hurt EC. In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p. Mol Biol Cell. 1997 Jan;8(1):33-46. PMID:9017593
  4. ↑ Kosova B, Pante N, Rollenhagen C, Hurt E. Nup192p is a conserved nucleoporin with a preferential location at the inner site of the nuclear membrane. J Biol Chem. 1999 Aug 6;274(32):22646-51. PMID:10428845
  5. ↑ Kosova B, Pante N, Rollenhagen C, Podtelejnikov A, Mann M, Aebi U, Hurt E. Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p. J Biol Chem. 2000 Jan 7;275(1):343-50. PMID:10617624
  6. ↑ Gomez-Ospina N, Morgan G, Giddings TH Jr, Kosova B, Hurt E, Winey M. Yeast nuclear pore complex assembly defects determined by nuclear envelope reconstruction. J Struct Biol. 2000 Oct;132(1):1-5. PMID:11121302 doi:10.1006/jsbi.2000.4305
  7. ↑ Fahrenkrog B, Aris JP, Hurt EC, Pante N, Aebi U. Comparative spatial localization of protein-A-tagged and authentic yeast nuclear pore complex proteins by immunogold electron microscopy. J Struct Biol. 2000 Apr;129(2-3):295-305. PMID:10806080 doi:http://dx.doi.org/10.1006/jsbi.2000.4223
  8. ↑ Bailer SM, Balduf C, Hurt E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol Cell Biol. 2001 Dec;21(23):7944-55. PMID:11689687 doi:http://dx.doi.org/10.1128/MCB.21.23.7944-7955.2001
  9. ↑ Lusk CP, Makhnevych T, Marelli M, Aitchison JD, Wozniak RW. Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes. J Cell Biol. 2002 Oct 28;159(2):267-78. Epub 2002 Oct 28. PMID:12403813 doi:10.1083/jcb.200203079
  10. ↑ Damelin M, Silver PA. In situ analysis of spatial relationships between proteins of the nuclear pore complex. Biophys J. 2002 Dec;83(6):3626-36. PMID:12496130 doi:http://dx.doi.org/S0006-3495(02)75363-0
  11. ↑ Gao H, Sumanaweera N, Bailer SM, Stochaj U. Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase Acc1p. J Biol Chem. 2003 Jul 11;278(28):25331-40. Epub 2003 May 1. PMID:12730220 doi:http://dx.doi.org/10.1074/jbc.M301607200
  12. ↑ Jeudy S, Schwartz TU. Crystal structure of nucleoporin Nic96 reveals a novel, intricate helical domain architecture. J Biol Chem. 2007 Nov 30;282(48):34904-12. Epub 2007 Sep 25. PMID:17897938 doi:10.1074/jbc.M705479200

2qx5, resolution 2.50Å

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