4IFQ

Crystal structure of Saccharomyces cerevisiae NUP192, residues 2 to 960 [ScNup192(2-960)]

Summary for 4IFQ

• Entry DOI: 10.2210/pdb4ifq/pdb
• Descriptor: Nucleoporin NUP192, SULFATE ION, IODIDE ION, ... (4 entities in total)
• Functional Keywords: structural genomics, nysgrc, psi-biology, new york structural genomics research consortium, alpha solenoid-like, nuclear pore complex component, npc, nup192, nup188, nucleoporin, protein transport, nucleocytoplasmic transport: a target for cellular control, npcxstals
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 113340.20

Authors

Sampathkumar, P.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC),Nucleocytoplasmic Transport: a Target for Cellular Control (NPCXstals) (deposition date: 2012-12-14, release date: 2013-02-20, Last modification date: 2024-10-16)

Primary citation

Sampathkumar, P.,Kim, S.J.,Upla, P.,Rice, W.J.,Phillips, J.,Timney, B.L.,Pieper, U.,Bonanno, J.B.,Fernandez-Martinez, J.,Hakhverdyan, Z.,Ketaren, N.E.,Matsui, T.,Weiss, T.M.,Stokes, D.L.,Sauder, J.M.,Burley, S.K.,Sali, A.,Rout, M.P.,Almo, S.C.
Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex.
Structure, 21:560-571, 2013

PubMed Abstract: The nuclear pore complex, composed of proteins termed nucleoporins (Nups), is responsible for nucleocytoplasmic transport in eukaryotes. Nuclear pore complexes (NPCs) form an annular structure composed of the nuclear ring, cytoplasmic ring, a membrane ring, and two inner rings. Nup192 is a major component of the NPC's inner ring. We report the crystal structure of Saccharomyces cerevisiae Nup192 residues 2-960 [ScNup192(2-960)], which adopts an α-helical fold with three domains (i.e., D1, D2, and D3). Small angle X-ray scattering and electron microscopy (EM) studies reveal that ScNup192(2-960) could undergo long-range transition between "open" and "closed" conformations. We obtained a structural model of full-length ScNup192 based on EM, the structure of ScNup192(2-960), and homology modeling. Evolutionary analyses using the ScNup192(2-960) structure suggest that NPCs and vesicle-coating complexes are descended from a common membrane-coating ancestral complex. We show that suppression of Nup192 expression leads to compromised nuclear transport and hypothesize a role for Nup192 in modulating the permeability of the NPC central channel.

PubMed: 23499021
DOI: 10.1016/j.str.2013.02.005

Experimental method

X-RAY DIFFRACTION (3.25 Å)