3GJX

Crystal Structure of the Nuclear Export Complex CRM1-Snurportin1-RanGTP

Summary for 3GJX

• Entry DOI: 10.2210/pdb3gjx/pdb
• Descriptor: Snurportin-1, GTP-binding nuclear protein Ran, Exportin-1, ... (8 entities in total)
• Functional Keywords: transport, cytoplasm, nucleus, rna-binding, acetylation, gtp-binding, host-virus interaction, nucleotide-binding, phosphoprotein, polymorphism, protein transport, mrna transport
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus: O95149 P62826; Cytoplasm (By similarity): Q6P5F9
• Total number of polymer chains: 6
• Total formula weight: 380015.03

Authors

Monecke, T.,Guettler, T.,Neumann, P.,Dickmanns, A.,Goerlich, D.,Ficner, R. (deposition date: 2009-03-09, release date: 2009-05-26, Last modification date: 2024-05-29)

Primary citation

Monecke, T.,Guttler, T.,Neumann, P.,Dickmanns, A.,Gorlich, D.,Ficner, R.
Crystal Structure of the Nuclear Export Receptor CRM1 in Complex with Snurportin1 and RanGTP.
Science, 2009

PubMed Abstract: CRM1 mediates nuclear export of numerous unrelated cargoes, which may carry a short leucine-rich nuclear export signal or export signatures that include folded domains. How CRM1 recognizes such a variety of cargoes has been unknown up to this point. Here we present the crystal structure of the SPN1.CRM1.RanGTP export complex at 2.5 angstrom resolution (where SPN1 is snurportin1 and RanGTP is guanosine 5' triphosphate-bound Ran). SPN1 is a nuclear import adapter for cytoplasmically assembled, m(3)G-capped spliceosomal U snRNPs (small nuclear ribonucleoproteins). The structure shows how CRM1 can specifically return the cargo-free form of SPN1 to the cytoplasm. The extensive contact area includes five hydrophobic residues at the SPN1 amino terminus that dock into a hydrophobic cleft of CRM1, as well as numerous hydrophilic contacts of CRM1 to m(3)G cap-binding domain and carboxyl-terminal residues of SPN1. The structure suggests that RanGTP promotes cargo-binding to CRM1 solely through long-range conformational changes in the exportin.

PubMed: 19389996
DOI: 10.1126/science.1173388

Experimental method

X-RAY DIFFRACTION (2.5 Å)