1b64

<StructureSection load='1b64' size='340' side='right'caption='[[1b64]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1b64]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B64 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b64 OCA], [https://pdbe.org/1b64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b64 RCSB], [https://www.ebi.ac.uk/pdbsum/1b64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b64 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/EF1B_HUMAN EF1B_HUMAN]] EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP.

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== Publication Abstract from PubMed ==

BACKGROUND: In eukaryotic protein synthesis, the multi-subunit elongation factor 1 (EF-1) plays an important role in ensuring the fidelity and regulating the rate of translation. EF-1alpha, which transports the aminoacyl tRNA to the ribosome, is a member of the G-protein superfamily. EF-1beta regulates the activity of EF-1alpha by catalyzing the exchange of GDP for GTP and thereby regenerating the active form of EF-1alpha. The structure of the bacterial analog of EF-1alpha, EF-Tu has been solved in complex with its GDP exchange factor, EF-Ts. These structures indicate a mechanism for GDP-GTP exchange in prokaryotes. Although there is good sequence conservation between EF-1alpha and EF-Tu, there is essentially no sequence similarity between EF-1beta and EF-Ts. We wished to explore whether the prokaryotic exchange mechanism could shed any light on the mechanism of eukaryotic translation elongation. RESULTS: Here, we report the structure of the guanine-nucleotide exchange factor (GEF) domain of human EF-1beta (hEF-1beta, residues 135-224); hEF-1beta[135-224], determined by nuclear magnetic resonance spectroscopy. Sequence conservation analysis of the GEF domains of EF-1 subunits beta and delta from widely divergent organisms indicates that the most highly conserved residues are in two loop regions. Intriguingly, hEF-1beta[135-224] shares structural homology with the GEF domain of EF-Ts despite their different primary sequences. CONCLUSIONS: On the basis of both the structural homology between EF-Ts and hEF-1beta[135-224] and the sequence conservation analysis, we propose that the mechanism of guanine-nucleotide exchange in protein synthesis has been conserved in prokaryotes and eukaryotes. In particular, Tyr181 of hEF-1beta[135-224] appears to be analogous to Phe81 of Escherichia coli EF-Ts.

The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli.,Perez JM, Siegal G, Kriek J, Hard K, Dijk J, Canters GW, Moller W Structure. 1999 Feb 15;7(2):217-26. PMID:10368288<ref>PMID:10368288</ref>

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

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== References ==

<references/>

[[Category: Human]]

[[Category: Canters, G W]]

[[Category: Dijk, J]]

[[Category: Hard, K]]

[[Category: Kriek, J]]

[[Category: Moller, W]]

[[Category: Perez, J M.J]]

[[Category: Siegal, G]]

[[Category: Translation elongation]]