2AHO
Structure of the archaeal initiation factor eIF2 alpha-gamma heterodimer from Sulfolobus solfataricus complexed with GDPNP
Summary for 2AHO
| Entry DOI | 10.2210/pdb2aho/pdb |
| Descriptor | Translation initiation factor 2 gamma subunit, Translation initiation factor 2 alpha subunit, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | initiation of translation, translation |
| Biological source | Sulfolobus solfataricus More |
| Total number of polymer chains | 2 |
| Total formula weight | 76762.30 |
| Authors | Yatime, L.,Mechulam, Y.,Blanquet, S.,Schmitt, E. (deposition date: 2005-07-28, release date: 2006-01-31, Last modification date: 2023-10-25) |
| Primary citation | Yatime, L.,Mechulam, Y.,Blanquet, S.,Schmitt, E. Structural Switch of the gamma Subunit in an Archaeal aIF2alphagamma Heterodimer Structure, 14:119-128, 2006 Cited by PubMed Abstract: Eukaryotic and archaeal initiation factors 2 (e/aIF2) are heterotrimeric proteins (alphabetagamma) supplying the small subunit of the ribosome with methionylated initiator tRNA. This study reports the crystallographic structure of an aIF2alphagamma heterodimer from Sulfolobus solfataricus bound to Gpp(NH)p-Mg(2+). aIF2gamma is in a closed conformation with the G domain packed on domains II and III. The C-terminal domain of aIF2alpha interacts with domain II of aIF2gamma. Conformations of the two switch regions involved in GTP binding are similar to those encountered in an EF1A:GTP:Phe-tRNA(Phe) complex. Comparison with the EF1A structure suggests that only the gamma subunit of the aIF2alphagamma heterodimer contacts tRNA. Because the alpha subunit markedly reinforces the affinity of tRNA for the gamma subunit, a contribution of the alpha subunit to the switch movements observed in the gamma structure is considered. PubMed: 16407071DOI: 10.1016/j.str.2005.09.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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