1dar
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dar FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dar OCA], [http://www.ebi.ac.uk/pdbsum/1dar PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dar RCSB]</span> | ||
}} | }} | ||
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[[Category: Liljas, A.]] | [[Category: Liljas, A.]] | ||
[[Category: Zheltonosova, J.]] | [[Category: Zheltonosova, J.]] | ||
| - | [[Category: GDP]] | ||
[[Category: ribosomal translocase]] | [[Category: ribosomal translocase]] | ||
[[Category: translational gtpase]] | [[Category: translational gtpase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:38:02 2008'' |
Revision as of 16:38, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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