5DLQ

Crystal structure of RanGTP-Exportin 4-eIF5A complex

Summary for 5DLQ

• Entry DOI: 10.2210/pdb5dlq/pdb
• Descriptor: Exportin-4, GTP-binding nuclear protein Ran, Eukaryotic translation initiation factor 5A-1, ... (5 entities in total)
• Functional Keywords: active transport, nuclear transport, nuclear export importin-beta family, exportin, heat repeat, gtpase, nucleotide binding, eif5a, translation factor, hypusine, unusual amino acid, protein transport
• Biological source: Mus musculus (Mouse); More
• Cellular location: Cytoplasm : Q9ESJ0 P63241; Nucleus: P62826
• Total number of polymer chains: 6
• Total formula weight: 324443.97

Authors

Aksu, M.,Trakhanov, S.,Gorlich, D. (deposition date: 2015-09-07, release date: 2016-06-22, Last modification date: 2024-10-16)

Primary citation

Aksu, M.,Trakhanov, S.,Gorlich, D.
Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A.
Nat Commun, 7:11952-11952, 2016

PubMed Abstract: Xpo4 is a bidirectional nuclear transport receptor that mediates nuclear export of eIF5A and Smad3 as well as import of Sox2 and SRY. How Xpo4 recognizes such a variety of cargoes is as yet unknown. Here we present the crystal structure of the RanGTP·Xpo4·eIF5A export complex at 3.2 Å resolution. Xpo4 has a similar structure as CRM1, but the NES-binding site is occluded, and a new interaction site evolved that recognizes both globular domains of eIF5A. eIF5A contains hypusine, a unique amino acid with two positive charges, which is essential for cell viability and eIF5A function in translation. The hypusine docks into a deep, acidic pocket of Xpo4 and is thus a critical element of eIF5A's complex export signature. This further suggests that Xpo4 recognizes other cargoes differently, and illustrates how Xpo4 suppresses - in a chaperone-like manner - undesired interactions of eIF5A inside nuclei.

PubMed: 27306458
DOI: 10.1038/ncomms11952

Experimental method

X-RAY DIFFRACTION (3.2 Å)