8T9L

Pom34-Pom152 membrane attachment site yeast NPC

Summary for 8T9L

• Entry DOI: 10.2210/pdb8t9l/pdb
• Related: 8TIE 8TJ5
• EMDB information: 41114 41116 41117 41119 41120 41121 41122 41123 41285 41300
• Descriptor: Nucleoporin POM152, Nucleoporin POM34 (2 entities in total)
• Functional Keywords: nuclear pore complex, nucleocytoplasmic transport, nucleoporin, membrane protein, translocase, transport protein
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 4
• Total formula weight: 372226.38

Authors

Akey, C.W.,Echeverria, I.,Ouch, C.,Fernandez-Martinez, J.,Rout, M.P. (deposition date: 2023-06-24, release date: 2023-10-11)

Primary citation

Akey, C.W.,Echeverria, I.,Ouch, C.,Nudelman, I.,Shi, Y.,Wang, J.,Chait, B.T.,Sali, A.,Fernandez-Martinez, J.,Rout, M.P.
Implications of a multiscale structure of the yeast nuclear pore complex.
Mol.Cell, 83:3283-3302.e5, 2023

PubMed Abstract: Nuclear pore complexes (NPCs) direct the nucleocytoplasmic transport of macromolecules. Here, we provide a composite multiscale structure of the yeast NPC, based on improved 3D density maps from cryogenic electron microscopy and AlphaFold2 models. Key features of the inner and outer rings were integrated into a comprehensive model. We resolved flexible connectors that tie together the core scaffold, along with equatorial transmembrane complexes and a lumenal ring that anchor this channel within the pore membrane. The organization of the nuclear double outer ring reveals an architecture that may be shared with ancestral NPCs. Additional connections between the core scaffold and the central transporter suggest that under certain conditions, a degree of local organization is present at the periphery of the transport machinery. These connectors may couple conformational changes in the scaffold to the central transporter to modulate transport. Collectively, this analysis provides insights into assembly, transport, and NPC evolution.

PubMed: 37738963
DOI: 10.1016/j.molcel.2023.08.025

Experimental method

ELECTRON MICROSCOPY (7 Å)