3QSY

Recognition of the methionylated initiator tRNA by the translation initiation factor 2 in Archaea

Summary for 3QSY

• Entry DOI: 10.2210/pdb3qsy/pdb
• Descriptor: Translation initiation factor 2 subunit gamma, Translation initiation factor 2 subunit alpha, tRNA, ... (5 entities in total)
• Functional Keywords: translation initiation, archaea, e/aif2, trnai, g-protein, gtp binding, met-trnai binding, ribosome binding, mrna binding, ribosome, translation-rna complex, translation/rna
• Biological source: Sulfolobus solfataricus; More
• Total number of polymer chains: 3
• Total formula weight: 81200.83

Authors

Nikonov, O.S.,Stolboushkina, E.A.,Zelinskaya, N.V.,Nikulin, A.D.,Garber, M.B.,Nikonov, S.V. (deposition date: 2011-02-22, release date: 2012-03-21, Last modification date: 2024-10-16)

Primary citation

Stolboushkina, E.,Nikonov, S.,Zelinskaya, N.,Arkhipova, V.,Nikulin, A.,Garber, M.,Nikonov, O.
Crystal structure of the archaeal translation initiation factor 2 in complex with a GTP analogue and Met-tRNAf(Met.)
J.Mol.Biol., 425:989-998, 2013

PubMed Abstract: Heterotrimeric aIF2αβγ (archaeal homologue of the eukaryotic translation initiation factor 2) in its GTP-bound form delivers Met-tRNAi(Met) to the small ribosomal subunit. It is known that the heterodimer containing the GTP-bound γ subunit and domain 3 of the α subunit of aIF2 is required for the formation of a stable complex with Met-tRNAi. Here, the crystal structure of an incomplete ternary complex including aIF2αD3γ⋅GDPNP⋅Met-tRNAf(Met) has been solved at 3.2Å resolution. This structure is in good agreement with biochemical and hydroxyl radical probing data. The analysis of the complex shows that despite the structural similarity of aIF2γ and the bacterial translation elongation factor EF-Tu, their modes of tRNA binding are very different. Remarkably, the recently published 5.0-Å-resolution structure of almost the same ternary initiation complex differs dramatically from the structure presented. Reasons for this discrepancy are discussed.

PubMed: 23291527
DOI: 10.1016/j.jmb.2012.12.023

Experimental method

X-RAY DIFFRACTION (3.2 Å)