5TVZ

Solution NMR structure of Saccharomyces cerevisiae Pom152 Ig-like repeat, residues 718-820

Summary for 5TVZ

• Entry DOI: 10.2210/pdb5tvz/pdb
• NMR Information: BMRB: 30201
• Descriptor: Nucleoporin POM152 (1 entity in total)
• Functional Keywords: nuclear pore complex, ig-like fold, nuclear envelope membrane, cadherin like fold, transport protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 12741.65

Authors

Dutta, K.,Sampathkumar, P.,Cowburn, D.,Almo, S.C.,Rout, M.P.,Fernandez-Martinez, J. (deposition date: 2016-11-10, release date: 2017-02-22, Last modification date: 2024-05-15)

Primary citation

Upla, P.,Kim, S.J.,Sampathkumar, P.,Dutta, K.,Cahill, S.M.,Chemmama, I.E.,Williams, R.,Bonanno, J.B.,Rice, W.J.,Stokes, D.L.,Cowburn, D.,Almo, S.C.,Sali, A.,Rout, M.P.,Fernandez-Martinez, J.
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex.
Structure, 25:434-445, 2017

PubMed Abstract: The membrane ring that equatorially circumscribes the nuclear pore complex (NPC) in the perinuclear lumen of the nuclear envelope is composed largely of Pom152 in yeast and its ortholog Nup210 (or Gp210) in vertebrates. Here, we have used a combination of negative-stain electron microscopy, nuclear magnetic resonance, and small-angle X-ray scattering methods to determine an integrative structure of the ∼120 kDa luminal domain of Pom152. Our structural analysis reveals that the luminal domain is formed by a flexible string-of-pearls arrangement of nine repetitive cadherin-like Ig-like domains, indicating an evolutionary connection between NPCs and the cell adhesion machinery. The 16 copies of Pom152 known to be present in the yeast NPC are long enough to form the observed membrane ring, suggesting how interactions between Pom152 molecules help establish and maintain the NPC architecture.

PubMed: 28162953
DOI: 10.1016/j.str.2017.01.006

Experimental method

SOLUTION NMR