4IFQ

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

4IFQ の概要

• エントリーDOI: 10.2210/pdb4ifq/pdb
• 分子名称: Nucleoporin NUP192, SULFATE ION, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 113340.20

構造登録者

Sampathkumar, P.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC),Nucleocytoplasmic Transport: a Target for Cellular Control (NPCXstals) (登録日: 2012-12-14, 公開日: 2013-02-20, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.25 Å)