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|1dar, resolution 2.40Å ()|
ELONGATION FACTOR G IN COMPLEX WITH GDP
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1dar is a 1 chain structure with sequence from Thermus thermophilus. The September 2006 RCSB PDB Molecule of the Month feature on Elongation Factors by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_9. Full crystallographic information is available from OCA.
- 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. 1996 May 15;4(5):555-65. PMID:8736554
- Park F, Gajiwala K, Eroshkina G, Furlong E, He D, Batiyenko Y, Romero R, Christopher J, Badger J, Hendle J, Lin J, Peat T, Buchanan S. Crystal structure of YIGZ, a conserved hypothetical protein from Escherichia coli k12 with a novel fold. Proteins. 2004 May 15;55(3):775-7. PMID:15103642 doi:10.1002/prot.20087