1dar

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[[Image:1dar.gif|left|200px]]
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[[Image:1dar.png|left|200px]]
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==Overview==
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{{ABSTRACT_8736554}}
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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.
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==About this Structure==
==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].
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].
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==Reference==
 
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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: Ribosomal translocase]]
[[Category: Ribosomal translocase]]
[[Category: Translational gtpase]]
[[Category: Translational gtpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:38:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:09:57 2008''

Revision as of 14:09, 26 June 2008

Image:1dar.png

Template:STRUCTURE 1dar

ELONGATION FACTOR G IN COMPLEX WITH GDP


Template:ABSTRACT 8736554

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.

Page seeded by OCA on Thu Jun 26 17:09:57 2008

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