1dar
From Proteopedia
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ELONGATION FACTOR G IN COMPLEX WITH GDP
Overview
BACKGROUND: 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. RESULTS:, The structure of EF-G-GDP has been refined at 2.4 A resolution. Comparison, with the nucleotide-free structure reveals that, upon GDP release, the, phosphate-binding loop (P-loop) adopts a closed conformation. This affects, the position of helix CG, the switch II loop and domains II, IV and V., Asp83 has a conformation similar to the conformation of the corresponding, residue in the EF-Tu/EF-Ts complex. The magnesium ion is absent in, EF-G-GDP. CONCLUSIONS: The results illustrate that conformational changes, in the P-loop can be transmitted to other parts of the structure. A, comparison of the structures of EF-G and EF-Tu suggests that EF-G, like, EF-Tu, undergoes a transition with domain rearrangements. The conformation, of EF-G-GDP around the nucleotide-binding site may be related to the, mechanism of nucleotide exchange.
About this Structure
1DAR is a Single protein structure of sequence from Thermus thermophilus with GDP as ligand. The following page contains interesting information on the relation of 1DAR with [Elongation Factors]. Full crystallographic information is available from OCA.
Reference
The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange., al-Karadaghi S, Aevarsson A, Garber M, Zheltonosova J, Liljas A, Structure. 1996 May 15;4(5):555-65. PMID:8736554
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