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1tui
From Proteopedia
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|PDB= 1tui |SIZE=350|CAPTION= <scene name='initialview01'>1tui</scene>, resolution 2.7Å | |PDB= 1tui |SIZE=350|CAPTION= <scene name='initialview01'>1tui</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tui OCA], [http://www.ebi.ac.uk/pdbsum/1tui PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tui RCSB]</span> | ||
}} | }} | ||
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[[Category: Polekhina, G.]] | [[Category: Polekhina, G.]] | ||
[[Category: Thirup, S.]] | [[Category: Thirup, S.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: MG]] | ||
[[Category: elongation factor]] | [[Category: elongation factor]] | ||
[[Category: gtp-binding]] | [[Category: gtp-binding]] | ||
[[Category: protein biosynthesis]] | [[Category: protein biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:14 2008'' |
Revision as of 21:01, 30 March 2008
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| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
INTACT ELONGATION FACTOR TU IN COMPLEX WITH GDP
Overview
BACKGROUND: Elongation factor Tu (EF-Tu) in its GTP conformation is a carrier of aminoacylated tRNAs (aa-tRNAs) to the ribosomal A site during protein biosynthesis. The ribosome triggers GTP hydrolysis, resulting in the dissociation of EF-Tu-GDP from the ribosome. The affinity of EF-Tu for other molecules involved in this process, some of which are unknown, is regulated by two regions (Switch I and Switch II) that have different conformations in the GTP and GDP forms. The structure of the GDP form of EF-Tu is known only as a trypsin-modified fragment, which lacks the Switch I, or effector, domain. The aim of this work was to establish the overall structure of intact EF-Tu-GDP, in particular the structure of the effector domain. RESULTS: The crystal structures of intact EF-Tu-GDP from Thermus aquaticus and Escherichia coli have been determined at resolutions of 2.7 A and 3.8 A, respectively. The structures confirm the domain orientation previously found in the structure of partially trypsin-digested EF-Tu-GDP. The structures of the effector region in T. aquaticus and E. coli EF-Tu-GDP are very similar. The C-terminal part of the effector region of EF-Tu-GDP is a beta hairpin; in EF-Tu-GTP, this region forms an alpha helix. This conformational change is not a consequence of crystal packing. CONCLUSIONS: EF-Tu undergoes major conformational changes upon GTP hydrolysis. Unlike other GTP-binding proteins, EF-Tu exhibits a dramatic conformational change in the effector region, involving an unwinding of a small helix and the formation of a beta hairpin structure. This change is presumably involved in triggering the release of tRNA, and EF-Tu, from the ribosome.
About this Structure
1TUI is a Single protein structure of sequence from Thermus aquaticus. The following page contains interesting information on the relation of 1TUI with [Elongation Factors]. Full crystallographic information is available from OCA.
Reference
Helix unwinding in the effector region of elongation factor EF-Tu-GDP., Polekhina G, Thirup S, Kjeldgaard M, Nissen P, Lippmann C, Nyborg J, Structure. 1996 Oct 15;4(10):1141-51. PMID:8939739
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