1b64: Difference between revisions
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==SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES== | ==SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES== | ||
<StructureSection load='1b64' size='340' side='right' caption='[[1b64]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1b64' size='340' side='right'caption='[[1b64]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b64]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B64 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1b64]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B64 FirstGlance]. <br> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/1b64_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/1b64_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1b64" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1b64" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Elongation factor 3D structures|Elongation factor 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Canters, G W]] | [[Category: Canters, G W]] | ||
[[Category: Dijk, J]] | [[Category: Dijk, J]] | ||
Revision as of 19:42, 28 August 2019
SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURESSOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES
Structural highlights
Function[EF1B_HUMAN] EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP. 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 PubMedBACKGROUND: 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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