1dar
From Proteopedia
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| - | [[Image:1dar.gif|left|200px]] | + | [[Image:1dar.gif|left|200px]] |
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| - | '''ELONGATION FACTOR G IN COMPLEX WITH GDP''' | + | {{Structure |
| + | |PDB= 1dar |SIZE=350|CAPTION= <scene name='initialview01'>1dar</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ELONGATION FACTOR G IN COMPLEX WITH GDP''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DAR is a [ | + | 1DAR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. The following page contains interesting information on the relation of 1DAR with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb81_1.html Elongation Factors]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DAR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8736554 8736554] |
[[Category: Elongation Factors]] | [[Category: Elongation Factors]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: translational gtpase]] | [[Category: translational gtpase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:35:29 2008'' |
Revision as of 08:35, 20 March 2008
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| , resolution 2.4Å | |||||||
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| 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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