1b64: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1b64.png|left|200px]]
-{{STRUCTURE_1b64|  PDB=1b64  |  SCENE=  }}
+==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]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1b64]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <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>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1b64 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES===
+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>
-{{ABSTRACT_PUBMED_10368288}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1b64" style="background-color:#fffaf0;"></div>
-[[1b64]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B64 OCA].
 ==See Also==
-*[[Elongation factor|Elongation factor]]
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:010368288</ref><ref group="xtra">PMID:015952781</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Canters, G W.]]
+[[Category: Large Structures]]
-[[Category: Dijk, J.]]
+[[Category: Canters GW]]
-[[Category: Hard, K.]]
+[[Category: Dijk J]]
-[[Category: Kriek, J.]]
+[[Category: Hard K]]
-[[Category: Moller, W.]]
+[[Category: Kriek J]]
-[[Category: Perez, J M.J.]]
+[[Category: Moller W]]
-[[Category: Siegal, G.]]
+[[Category: Perez JMJ]]
-[[Category: G-protein]]
+[[Category: Siegal G]]
-[[Category: Guanine nucleotide exchange factor]]
-[[Category: Translation elongation]]