View source for 1dar

[[Image:1dar.gif|left|200px]]

 {{Structure
|PDB= 1dar |SIZE=350|CAPTION= <scene name='initialview01'>1dar</scene>, resolution 2.4&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
|ACTIVITY= 
|GENE= 
}}

'''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 [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==
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: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Aevarsson, A.]]
[[Category: Al-Karadaghi, S.]]
[[Category: Garber, M.]]
[[Category: Liljas, A.]]
[[Category: Zheltonosova, J.]]
[[Category: GDP]]
[[Category: ribosomal translocase]]
[[Category: translational gtpase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:29:16 2008''