PDBsum entry 4c0s

Translation

PDB id: 4c0s

Contents

Protein chains

451 a.a.

Ligands

GDP ×2

Metals

_MG ×2

Waters ×9

PDB id:

4c0s

Name:

Translation

Title:

Mammalian translation elongation factor eef1a2

Structure:

Elongation factor 1-alpha 2. Chain: a, b. Synonym: ef-1-alpha-2, eukaryotic elongation factor 1 a-2, eef1a-2, statin-s1

Source:

Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Tissue: muscle

Resolution:

2.70Å R-factor: 0.205 R-free: 0.256

Authors:

T.Crepin,V.F.Shalak,A.D.Yaremchuk,D.O.Vlasenko,A.A.Mccarthy, B.S.Negrutskii,M.A.Tukalo,A.V.El'Skaya

Key ref:

T.Crepin et al. (2014). Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes. Nucleic Acids Res, 42, 12939-12948. PubMed id: 25326326 DOI: 10.1093/nar/gku974

Date:

07-Aug-13 Release date: 27-Aug-14

Protein chains

Q71V39  (EF1A2_RABIT) -  Elongation factor 1-alpha 2 from Oryctolagus cuniculus

Seq: 463 a.a.

Struc: 451 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1093/nar/gku974

Nucleic Acids Res 42:12939-12948 (2014)

PubMed id: 25326326

Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.

T.Crepin, V.F.Shalak, A.D.Yaremchuk, D.O.Vlasenko, A.McCarthy, B.S.Negrutskii, M.A.Tukalo, A.V.El'skaya.

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.