Archaeal initiation factor 2 (aIF2) in its GTP-bound form binds methionylated initiator tRNA to form a ternary initiation complex. Its 3D structure, as determined by crystallography and small-angle X-ray scattering analysis, reveals that despite the structural homology between aIF2 and elongation factor EF1A, these two G proteins of the translation apparatus use very different tRNA-binding strategies.
- Emmanuelle Schmitt
- Michel Panvert
- Yves Mechulam
