1eft

<table><tr><td colspan='2'>[[1eft]] is a 1 chain structure. 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=1EFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EFT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</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=1eft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eft OCA], [http://pdbe.org/1eft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1eft RCSB], [http://www.ebi.ac.uk/pdbsum/1eft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1eft ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/EFTU_THEAQ 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]

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== Publication Abstract from PubMed ==

BACKGROUND: Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected. RESULTS: The crystal structure of EF-Tu from Thermus aquaticus, complexed to the GTP analogue GDPNP, has been determined at 2.5 A resolution and compared to the structure of Escherichia coli EF-Tu.GDP. During the transition from the GDP (inactive) to the GTP (active) form, domain 1, containing the GTP-binding site, undergoes internal conformational changes similar to those observed in ras-p21. In addition, a dramatic rearrangement of domains is observed, corresponding to a rotation of 90.8 degrees of domain 1 relative to domains 2 and 3. Residues that are affected in the binding of aminoacyl-tRNA are found in or near the cleft formed by the domain interface. CONCLUSION: GTP binding by EF-Tu leads to dramatic conformational changes which expose the tRNA binding site. It appears that tRNA binding to EF-Tu induces a further conformational change, which may affect the GTPase activity.

The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.,Kjeldgaard M, Nissen P, Thirup S, Nyborg J Structure. 1993 Sep 15;1(1):35-50. PMID:8069622<ref>PMID:8069622</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1eft" style="background-color:#fffaf0;"></div>

*[[Elongation factor|Elongation factor]]

[[Category: Kjeldgaard, M]]

[[Category: Nissen, P]]

[[Category: Nyborg, J]]

[[Category: Thirup, S]]

[[Category: Elongation factor]]