1DAR
ELONGATION FACTOR G IN COMPLEX WITH GDP
Summary for 1DAR
Entry DOI | 10.2210/pdb1dar/pdb |
Descriptor | ELONGATION FACTOR G, GUANOSINE-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | ribosomal translocase, translational gtpase |
Biological source | Thermus thermophilus |
Cellular location | Cytoplasm: Q5SHN5 |
Total number of polymer chains | 1 |
Total formula weight | 77420.30 |
Authors | Al-Karadaghi, S.,Aevarsson, A.,Garber, M.,Zheltonosova, J.,Liljas, A. (deposition date: 1996-02-15, release date: 1996-07-11, Last modification date: 2024-02-07) |
Primary citation | al-Karadaghi, S.,Aevarsson, A.,Garber, M.,Zheltonosova, J.,Liljas, A. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure, 4:555-565, 1996 Cited by PubMed Abstract: Elongation factor G (EF-G) catalyzes the translocation step of translation. During translocation EF-G passes through four main conformational states: the GDP complex, the nucleotide-free state, the GTP complex, and the GTPase conformation. The first two of these conformations have been previously investigated by crystallographic methods. PubMed: 8736554DOI: 10.1016/S0969-2126(96)00061-5 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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