EF-Ts

EF-Ts comprises the majority of the top portion of the protein, while EF-Tu makes up the bottom half where the beta barrels are seen.

Therefore, EF-Ts main role is recycling EF-Tu back to its active state in order to complete another elongation cycle.

The majority of this pathway is performed through conformational changes of EF-Tu domain 1 which contains the active site and manipulation of the switch 1 & 2 regions by the ribosome and tRNA.

Mutation of Leu148 and Glu 152 decreased the rate at which EF-Ts N-terminal domain binds to Helix D significantly, concluding these two residues play an important role in the reaction pathway.

EF-Ts belongs both to the group of proteins known as guanine nucleotide exchange factors, found in many different biochemical pathways, and also to the tsf superfamily.

The majority of the amino acid conservation seen between other organisms is located in the N-terminal domain where EF-Ts bind to EF-Tu and the guanine nucleotide exchange occurs.

In eukaryotes, EF-1 performs the same function, and the mechanism for guanine nucleotide exchange is nearly identical as for EF-Ts despite the structural dissimilarities between the two elongation factors.