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translation elongation factor EFG/EF2
Also known as Transl_elong_EFG/EF2, IPR004540, EF-G, Elongation factor G
EF-G (elongation factor G, historically known as translocase) is a prokaryotic elongation factor involved in mRNA translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.
Key facts
- Enzyme.AltNames
- Elongation factor G, EF-G
- Enzyme.name
- Protein-synthesizing GTPase
- Enzyme.image
- EF-G Post State PDB 4V5F.jpg
- Enzyme.image_size
- 200px
- Enzyme.EC_number
- 3.6.5.3
via Wikipedia infobox
Article
12 sectionsContents
- Structure
- EF-G on the ribosome
- Binding to L7/L12
- Interaction with the GTPase Associated Center
- Function in protein elongation
- Function in protein termination
- Clinical significance
- Evolution
- See also
- References
- Further reading
- External links
EF-G (elongation factor G, historically known as translocase) is a prokaryotic elongation factor involved in mRNA translation. As a GTPase, EF-G catalyzes the movement (translocation) of transfer RNA (tRNA) and messenger RNA (mRNA) through the ribosome.
== Structure == Encoded by the fusA gene on the str operon, EF-G is made up of 704 amino acids that form 5 domains, labeled Domain I through Domain V. Domain I may be referred to as the G-domain or as Domain I(G), since it binds to and hydrolyzes guanosine triphosphate (GTP). Domain I also helps EF-G bind to the ribosome, and contains the N-terminal of the polypeptide chain. Domain IV is important for translocation, as it undergoes a significant conformational change and enters the A site on the 30S ribosomal subunit, pushing the mRNA and tRNA molecules from the A site to the P site.