4C0S

Mammalian translation elongation factor eEF1A2

Summary for 4C0S

• Entry DOI: 10.2210/pdb4c0s/pdb
• Descriptor: ELONGATION FACTOR 1-ALPHA 2, GUANOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: translation
• Biological source: ORYCTOLAGUS CUNICULUS (RABBIT)
• Cellular location: Nucleus : Q71V39
• Total number of polymer chains: 2
• Total formula weight: 102345.13

Authors

Crepin, T.,Shalak, V.F.,Yaremchuk, A.D.,Vlasenko, D.O.,McCarthy, A.A.,Negrutskii, B.S.,Tukalo, M.A.,El'skaya, A.V. (deposition date: 2013-08-07, release date: 2014-08-27, Last modification date: 2024-11-20)

Primary citation

Crepin, T.,Mccarthy, A.,Negrutskii, A.,Shalak, V.F.,Tukalo, V.,Vlasenko, D.O.,Yaremchuk, A.D.
Mammalian Translation Elongation Factor Eef1A2: X-Ray Structure and New Features of Gdp/GTP Exchange Mechanism in Higher Eukaryotes
Nucleic Acids Res., 42:12939-, 2014

PubMed 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.

PubMed: 25326326
DOI: 10.1093/NAR/GKU974

Experimental method

X-RAY DIFFRACTION (2.703 Å)