1f60

<table><tr><td colspan='2'>[[1f60]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F60 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b64|1b64]]</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=1f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f60 OCA], [http://pdbe.org/1f60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f60 RCSB], [http://www.ebi.ac.uk/pdbsum/1f60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f60 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/EF1B_YEAST EF1B_YEAST]] Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation of eEF1A-GTP, which rapidly forms a ternary complex with aminoacyl-tRNA that in turn displaces eEF1B from the complex.<ref>PMID:10409717</ref>

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== Publication Abstract from PubMed ==

The crystal structure of a complex between the protein biosynthesis elongation factor eEF1A (formerly EF-1alpha) and the catalytic C terminus of its exchange factor, eEF1Balpha (formerly EF-1beta), was determined to 1.67 A resolution. One end of the nucleotide exchange factor is buried between the switch 1 and 2 regions of eEF1A and destroys the binding site for the Mg(2+) ion associated with the nucleotide. The second end of eEF1Balpha interacts with domain 2 of eEF1A in the region hypothesized to be involved in the binding of the CCA-aminoacyl end of the tRNA. The competition between eEF1Balpha and aminoacylated tRNA may be a central element in channeling the reactants in eukaryotic protein synthesis. The recognition of eEF1A by eEF1Balpha is very different from that observed in the prokaryotic EF-Tu:EF-Ts complex. Recognition of the switch 2 region in nucleotide exchange is, however, common to the elongation factor complexes and those of Ras:Sos and Arf1:Sec7.

Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.,Andersen GR, Pedersen L, Valente L, Chatterjee I, Kinzy TG, Kjeldgaard M, Nyborg J Mol Cell. 2000 Nov;6(5):1261-6. PMID:11106763<ref>PMID:11106763</ref>

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

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== References ==

<references/>

[[Category: Atcc 18824]]

[[Category: Andersen, G R]]

[[Category: Kinzy, T G]]

[[Category: Nyborg, J]]

[[Category: Pedersen, L]]

[[Category: Valente, L]]

[[Category: Translation]]