Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice.

Publication Type:

Journal Article

Authors:

Brohawn, Stephen G; Schwartz, Thomas U

Source:

Nat Struct Mol Biol, Volume 16, Issue 11, p.1173-7 (2009)

Keywords:

Crystallography, X-Ray, Humans, Models, Biological, Models, Molecular, Nuclear Pore, Nuclear Pore Complex Proteins, Protein Binding, Protein Multimerization, Saccharomyces cerevisiae Proteins

Abstract:

<p>Nuclear pore complexes (NPCs) facilitate all nucleocytoplasmic transport. These massive protein assemblies are modular, with a stable structural scaffold supporting more dynamically attached components. The scaffold is made from multiple copies of the heptameric Y complex and the heteromeric Nic96 complex. We previously showed that members of these core subcomplexes specifically share an ACE1 fold with Sec31 of the COPII vesicle coat, and we proposed a lattice model for the NPC based on this commonality. Here we present the crystal structure of the heterotrimeric 134-kDa complex of Nup84-Nup145C-Sec13 of the Y complex. The heterotypic ACE1 interaction of Nup84 and Nup145C is analogous to the homotypic ACE1 interaction of Sec31 that forms COPII lattice edge elements and is inconsistent with the alternative 'fence-like' NPC model. We construct a molecular model of the Y complex and compare the architectural principles of COPII and NPC lattices.</p>