4FCC

Glutamate dehydrogenase from E. coli

Summary for 4FCC

• Entry DOI: 10.2210/pdb4fcc/pdb
• Related: 4FHL 4FHM 4FHN
• Descriptor: Glutamate dehydrogenase (2 entities in total)
• Functional Keywords: protein complex, rossmann fold, metabolic role, nad, nadp, oxidoreductase
• Biological source: Escherichia coli O157:H7
• Total number of polymer chains: 12
• Total formula weight: 586372.87

Authors

Bilokapic, S.,Schwartz, T.U. (deposition date: 2012-05-24, release date: 2012-09-26, Last modification date: 2024-02-28)

Primary citation

Bilokapic, S.,Schwartz, T.U.
Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex.
Proc.Natl.Acad.Sci.USA, 109:15241-15246, 2012

PubMed Abstract: Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous assemblies composed of multiple copies of ~30 different proteins called nucleoporins. To unravel the basic scaffold underlying the NPC, we have characterized the species-specific scaffold nucleoporin Nup37 and ELY5/ELYS. Both proteins integrate directly via Nup120/160 into the universally conserved heptameric Y-complex, the critical unit for the assembly and functionality of the NPC. We present the crystal structure of Schizosaccharomyces pombe Nup37 in complex with Nup120, a 174-kDa subassembly that forms one of the two short arms of the Y-complex. Nup37 binds near the bend of the L-shaped Nup120 protein, potentially stabilizing the relative orientation of its two domains. By means of reconstitution assays, we pinpoint residues crucial for this interaction. In vivo and in vitro results show that ELY5 binds near an interface of the Nup120-Nup37 complex. Complementary biochemical and cell biological data refine and consolidate the interactions of Nup120 within the current Y-model. Finally, we propose an orientation of the Y-complex relative to the pore membrane, consistent with the lattice model.

PubMed: 22955883
DOI: 10.1073/pnas.1205151109

Experimental method

X-RAY DIFFRACTION (2 Å)