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1tui

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Revision as of 15:53, 11 September 2015

INTACT ELONGATION FACTOR TU IN COMPLEX WITH GDP

Structural highlights

1tui is a 3 chain structure with sequence from Thermus aquaticus. The September 2006 RCSB PDB Molecule of the Month feature on Elongation Factors by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[EFTU_THEAQ] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118_B]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Polekhina G, Thirup S, Kjeldgaard M, Nissen P, Lippmann C, Nyborg J. Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Structure. 1996 Oct 15;4(10):1141-51. PMID:8939739

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tui"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1tui]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. The September 2006 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Elongation Factors''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2006_9 10.2210/rcsb_pdb/mom_2006_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TUI FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1tui RCSB], [http://www.ebi.ac.uk/pdbsum/1tui PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1tui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tui RCSB], [http://www.ebi.ac.uk/pdbsum/1tui PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1tui" style="background-color:#fffaf0;"></div>
 ==See Also==

1tui

From Proteopedia

Revision as of 15:53, 11 September 2015

INTACT ELONGATION FACTOR TU IN COMPLEX WITH GDP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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