This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1dar

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dar.gif|left|200px]]
+
[[Image:1dar.png|left|200px]]
<!--
<!--
Line 12: Line 12:
-
==Overview==
+
{{ABSTRACT_8736554}}
-
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==
==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].
- 
-
==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: Elongation Factors]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 30: Line 26:
[[Category: Ribosomal translocase]]
[[Category: Ribosomal translocase]]
[[Category: Translational gtpase]]
[[Category: Translational gtpase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:38:16 2008''
+
 
 +
''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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dar"
Personal tools