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TitleStructure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex.
Journal, issue, pagesStructure, Vol. 21, Issue 4, Page 560-571, Year 2013
Publish dateApr 2, 2013
AuthorsParthasarathy Sampathkumar / Seung Joong Kim / Paula Upla / William J Rice / Jeremy Phillips / Benjamin L Timney / Ursula Pieper / Jeffrey B Bonanno / Javier Fernandez-Martinez / Zhanna Hakhverdyan / Natalia E Ketaren / Tsutomu Matsui / Thomas M Weiss / David L Stokes / J Michael Sauder / Stephen K Burley / Andrej Sali / Michael P Rout / Steven C Almo /
PubMed AbstractThe nuclear pore complex, composed of proteins termed nucleoporins (Nups), is responsible for nucleocytoplasmic transport in eukaryotes. Nuclear pore complexes (NPCs) form an annular structure ...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.
External linksStructure / PubMed:23499021 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.25 - 26.0 Å
Structure data

EMDB-5556:
Negative stain electron microscopy structure of Nup192
Method: EM (single particle) / Resolution: 26.0 Å

PDB-4ifq:
Crystal structure of Saccharomyces cerevisiae NUP192, residues 2 to 960 [ScNup192(2-960)]
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

Chemicals

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-IOD:
IODIDE ION / Iodide

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsPROTEIN TRANSPORT / Structural genomics / NYSGRC / PSI-Biology / New York Structural Genomics Research Consortium / alpha solenoid-like / Nuclear Pore Complex component / NPC / Nup192 / Nup188 / Nucleoporin / Nucleocytoplasmic Transport: a Target for Cellular Control / NPCXstals

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