5MSE

GFP nuclear transport receptor mimic 3B8

Summary for 5MSE

• Entry DOI: 10.2210/pdb5mse/pdb
• Descriptor: Green fluorescent protein, SODIUM ION, IMIDAZOLE, ... (4 entities in total)
• Functional Keywords: gfp nuclear transport receptor, fluorescent protein
• Biological source: Aequorea victoria
• Total number of polymer chains: 4
• Total formula weight: 110856.63

Authors

Huyton, T.,Gorlich, D. (deposition date: 2017-01-04, release date: 2018-05-02, Last modification date: 2024-11-20)

Primary citation

Frey, S.,Rees, R.,Schunemann, J.,Ng, S.C.,Funfgeld, K.,Huyton, T.,Gorlich, D.
Surface Properties Determining Passage Rates of Proteins through Nuclear Pores.
Cell, 174:202-217.e9, 2018

PubMed Abstract: Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport through an FG domain-controlled barrier. We now explore how surface-features of a mobile species determine its NPC passage rate. Negative charges and lysines impede passage. Hydrophobic residues, certain polar residues (Cys, His), and, surprisingly, charged arginines have striking translocation-promoting effects. Favorable cation-π interactions between arginines and FG-phenylalanines may explain this apparent paradox. Application of these principles to redesign the surface of GFP resulted in variants that show a wide span of transit rates, ranging from 35-fold slower than wild-type to ∼500 times faster, with the latter outpacing even naturally occurring nuclear transport receptors (NTRs). The structure of a fast and particularly FG-specific GFP variant illustrates how NTRs can expose multiple regions for binding hydrophobic FG motifs while evading non-specific aggregation. Finally, we document that even for NTR-mediated transport, the surface-properties of the "passively carried" cargo can strikingly affect the translocation rate.

PubMed: 29958108
DOI: 10.1016/j.cell.2018.05.045

Experimental method

X-RAY DIFFRACTION (1.66 Å)