1gh8: Difference between revisions

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-[[Image:1gh8.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1gh8", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1gh8|  PDB=1gh8  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM'''
+==SOLUTION STRUCTURE OF THE ARCHAEAL TRANSLATION ELONGATION FACTOR 1BETA FROM METHANOBACTERIUM THERMOAUTOTROPHICUM==
+<StructureSection load='1gh8' size='340' side='right'caption='[[1gh8]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1gh8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1d5k 1d5k]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GH8 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=1gh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gh8 OCA], [https://pdbe.org/1gh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gh8 RCSB], [https://www.ebi.ac.uk/pdbsum/1gh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gh8 ProSAT], [https://www.topsan.org/Proteins/NESGC/1gh8 TOPSAN]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EF1B_METTH EF1B_METTH] Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA.
+== 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/gh/1gh8_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=1gh8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The tertiary fold of the elongation factor, aEF-1beta, from Methanobacterium thermoautotrophicum was determined in a high-throughput fashion using a minimal set of NMR experiments. NMR secondary structure prediction, deuterium exchange experiments and the analysis of chemical shift perturbations were combined to identify the protein fold as an alpha-beta sandwich typical of many RNA binding proteins including EF-G. Following resolution of the tertiary fold, a high resolution structure of aEF-1beta was determined using heteronuclear and homonuclear NMR experiments and a semi-automated NOESY assignment strategy. Analysis of the aEF-1beta structure revealed close similarity to its human analogue, eEF-1beta. In agreement with studies on EF-Ts and human EF-1beta, a functional mechanism for nucleotide exchange is proposed wherein Phe46 on an exposed loop acts as a lever to eject GDP from the associated elongation factor G-protein, aEF-1alpha. aEF-1beta was also found to bind calcium in the groove between helix alpha2 and strand beta4. This novel feature was not observed previously and may serve a structural function related to protein stability or may play a functional role in archaeal protein translation.
-==Overview==
+Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum.,Kozlov G, Ekiel I, Beglova N, Yee A, Dharamsi A, Engel A, Siddiqui N, Nong A, Gehring K J Biomol NMR. 2000 Jul;17(3):187-94. PMID:10959626<ref>PMID:10959626</ref>
-The tertiary fold of the elongation factor, aEF-1beta, from Methanobacterium thermoautotrophicum was determined in a high-throughput fashion using a minimal set of NMR experiments. NMR secondary structure prediction, deuterium exchange experiments and the analysis of chemical shift perturbations were combined to identify the protein fold as an alpha-beta sandwich typical of many RNA binding proteins including EF-G. Following resolution of the tertiary fold, a high resolution structure of aEF-1beta was determined using heteronuclear and homonuclear NMR experiments and a semi-automated NOESY assignment strategy. Analysis of the aEF-1beta structure revealed close similarity to its human analogue, eEF-1beta. In agreement with studies on EF-Ts and human EF-1beta, a functional mechanism for nucleotide exchange is proposed wherein Phe46 on an exposed loop acts as a lever to eject GDP from the associated elongation factor G-protein, aEF-1alpha. aEF-1beta was also found to bind calcium in the groove between helix alpha2 and strand beta4. This novel feature was not observed previously and may serve a structural function related to protein stability or may play a functional role in archaeal protein translation.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-GH8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1d5k 1d5k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH8 OCA].
+</div>
+<div class="pdbe-citations 1gh8" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Rapid fold and structure determination of the archaeal translation elongation factor 1beta from Methanobacterium thermoautotrophicum., Kozlov G, Ekiel I, Beglova N, Yee A, Dharamsi A, Engel A, Siddiqui N, Nong A, Gehring K, J Biomol NMR. 2000 Jul;17(3):187-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10959626 10959626]
+*[[Elongation factor 3D structures|Elongation factor 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Methanothermobacter thermautotrophicus]]
-[[Category: Single protein]]
+[[Category: Ekiel I]]
-[[Category: Ekiel, I.]]
+[[Category: Gehring K]]
-[[Category: Gehring, K.]]
+[[Category: Kozlov G]]
-[[Category: Kozlov, G.]]
-[[Category: NESG, Northeast Structural Genomics Consortium.]]
-[[Category: Alpha-beta sandwich]]
-[[Category: Gene regulation]]
-[[Category: Nesg]]
-[[Category: Northeast structural genomics consortium]]
-[[Category: Protein structure initiative]]
-[[Category: Psi]]
-[[Category: Structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:33:26 2008''