PDBsum entry 4c0s

Translation

PDB id: 4c0s

Contents

Protein chains

451 a.a.

Ligands

GDP ×2

Metals

_MG ×2

Waters ×9

References listed in PDB file

Key reference

• Title: Mammalian translation elongation factor eef1a2: X-Ray structure and new features of gdp/gtp exchange mechanism in higher eukaryotes.
• Authors: T.Crepin, V.F.Shalak, A.D.Yaremchuk, D.O.Vlasenko, A.Mccarthy, B.S.Negrutskii, M.A.Tukalo, A.V.El'Skaya.
• Ref.: Nucleic Acids Res, 2014, 42, 12939-12948. [DOI no: 10.1093/nar/gku974]
• PubMed id: 25326326

Abstract

Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during the ribosomal polypeptide chain elongation. eEF1A*GTP establishes a complex with the aminoacyl-tRNA in the A site of the 80S ribosome. Correct codon-anticodon recognition triggers GTP hydrolysis, with subsequent dissociation of eEF1A*GDP from the ribosome. The structures of both the 'GTP'- and 'GDP'-bound conformations of eEF1A are unknown. Thus, the eEF1A-related ribosomal mechanisms were anticipated only by analogy with the bacterial homolog EF-Tu. Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis.