Elongation factor G
Also known as: fus, fusA
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Classification
- Family (Pfam)
- PF00679 EFG_C, PF14492 EFG_III, PF03764 EFG_IV, PF00009 GTP_EFTU, PF03144 GTP_EFTU_D2
- InterPro
- EFG_II, EFG_III, EFG_III/V, EFG_IV, EFG_V, EFG_V-like, EFTu-like_2, G_TR_CS, P-loop_NTPase, Ribosomal_Su5_D2-typ_SF, Ribsml_uS5_D2-typ_fold_subgr, Small_GTP-bd, T_Tr_GTP-bd_dom, Transl_B-barrel_sf, Transl_elong_EFG/EF2, Transl_elong_EFG/EF2_IV
- Functional cluster
- GroEL/Cpn60 Chaperonins
Experimental structures · PDB · 4
A predicted model is available from AlphaFold.
Gene Ontology · 5
Drugs targeting this protein · 2
- FUSIDATE SODIUM inhibitor
- FUSIDIC ACID inhibitor
Related proteins · sequence + function similarity
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
- Elongation factor G 1.00
Literature · 1 cited papers
- Biological cost and compensatory evolution in fusidic acid-resistant Staphylococcus aureus. Mol. Microbiol. · 2001
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