PROSITE documentation PDOC01001

Elongation factor 1 (EF-1) gamma C-terminal domain profile

Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes [1]. EF-1 is composed of four subunits: the α chain which binds GTP and aminoacyl-tRNAs, the γ chain that probably plays a role in anchoring the complex to other cellular components and the β and delta (or β') chains. The γ chain is a protein of about 410 to 440 residues, which consists of two independent domains, a glutathione S-transferase (GST) homologous N-terminal region responsible for the interaction with EF-1 α and a highly conserved exceptionally protease resistant ~160 residue C-terminal domain [2].

The structure of the EF-1 γ C-terminal domain consists of a five-stranded antiparallel β-sheet surrounded by five α-helices and resembles a contact lens (see <PDB:1PBU>). The EF-1 γ C-terminal domain contains an usually high number of aromatic amino acids. These residues pack together in two clusters, which are located on opposite faces of the central β-sheet. The distribution of the surface-exposed, conserved residues in the EF-1 γ C-terminal domain is highly asymmetric. The concave surface and part of the edge surrounding it contain the majority of the conserved amino acids whereas the convex surface is relatively poorly conserved. It has been suggested that the concave face of the EF-1 γ C-terminal domain might be involved in some biologically relevant interface(s) [2].

The profile we developed covers the entire EF-1 γ C-terminal domain.