1EJ1

COCRYSTAL STRUCTURE OF THE MESSENGER RNA 5' CAP-BINDING PROTEIN (EIF4E) BOUND TO 7-METHYL-GDP

Summary for 1EJ1

• Entry DOI: 10.2210/pdb1ej1/pdb
• Related: 1EJ4
• Descriptor: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E, 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: protein 5' mrna cap complex, translation
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 45206.70

Authors

Marcotrigiano, J.,Gingras, A.-C.,Sonenberg, N.,Burley, S.K. (deposition date: 2000-02-29, release date: 2000-03-15, Last modification date: 2024-03-06)

Primary citation

Marcotrigiano, J.,Gingras, A.C.,Sonenberg, N.,Burley, S.K.
Cocrystal structure of the messenger RNA 5' cap-binding protein (eIF4E) bound to 7-methyl-GDP.
Cell(Cambridge,Mass.), 89:951-961, 1997

PubMed Abstract: The X-ray structure of the eukaryotic translation initiation factor 4E (eIF4E), bound to 7-methyl-GDP, has been determined at 2.2 A resolution. eIF4E recognizes 5' 7-methyl-G(5')ppp(5')N mRNA caps during the rate-limiting initiation step of translation. The protein resembles a cupped hand and consists of a curved, 8-stranded antiparallel beta sheet, backed by three long alpha helices. 7-methyl-GDP binds in a narrow cap-binding slot on the molecule's concave surface, where 7-methyl-guanine recognition is mediated by base sandwiching between two conserved tryptophans, plus formation of three hydrogen bonds and a van der Waals contact between its N7-methyl group and a third conserved tryptophan. The convex dorsal surface of the molecule displays a phylogenetically conserved hydrophobic/acidic portion, which may interact with other translation initiation factors and regulatory proteins.

PubMed: 9200613
DOI: 10.1016/S0092-8674(00)80280-9

Experimental method

X-RAY DIFFRACTION (2.2 Å)