4fhm | pdb_00004fhm

Nup37-Nup120(aa1-961) complex from Schizosaccharomyces pombe

spinqualitylabelsall models 4fhm, resolution 4.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fhm is a 2 chain structure with sequence from Fission yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4fhl, 4fhn, 4fcc Gene: Nup37, SPAC4F10.18 (Fission yeast), nup120, SPBC3B9.16c (Fission yeast) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NU120_SCHPO] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. Publication Abstract from PubMed Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous assemblies composed of multiple copies of approximately 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. Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex.,Bilokapic S, Schwartz TU Proc Natl Acad Sci U S A. 2012 Sep 18;109(38):15241-6. Epub 2012 Sep 5. PMID:22955883 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nucleoporin

Proteopedia Page Contributors and Editors (what is this?)

OCA