1jny: Difference between revisions

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<StructureSection load='1jny' size='340' side='right'caption='[[1jny]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1jny' size='340' side='right'caption='[[1jny]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jny]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JNY FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jny]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JNY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></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=1jny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jny OCA], [https://pdbe.org/1jny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jny RCSB], [https://www.ebi.ac.uk/pdbsum/1jny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jny ProSAT]</span></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=1jny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jny OCA], [https://pdbe.org/1jny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jny RCSB], [https://www.ebi.ac.uk/pdbsum/1jny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jny ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/EF1A_SULSO EF1A_SULSO]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.  
[https://www.uniprot.org/uniprot/EF1A_SACS2 EF1A_SACS2] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1jny ConSurf].
</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=1jny ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of elongation factor 1alpha from the archaeon Sulfolobus solfataricus in complex with GDP (SsEF-1alpha.GDP) at 1.8 A resolution is reported. As already known for the eubacterial elongation factor Tu, the SsEF-1alpha.GDP structure consists of three different structural domains. Surprisingly, the analysis of the GDP-binding site reveals that the nucleotide- protein interactions are not mediated by Mg(2+). Furthermore, the residues that usually co-ordinate Mg(2+) through water molecules in the GTP-binding proteins, though conserved in SsEF-1alpha, are located quite far from the binding site. [(3)H]GDP binding experiments confirm that Mg(2+) has only a marginal effect on the nucleotide exchange reaction of SsEF-1alpha, although essential to GTPase activity elicited by SsEF-1alpha. Finally, structural comparisons of SsEF- 1alpha.GDP with yeast EF-1alpha in complex with the nucleotide exchange factor EF-1beta shows that a dramatic rearrangement of the overall structure of EF-1alpha occurs during the nucleotide exchange.
The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange.,Vitagliano L, Masullo M, Sica F, Zagari A, Bocchini V EMBO J. 2001 Oct 1;20(19):5305-11. PMID:11574461<ref>PMID:11574461</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jny" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 35091]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bocchini, V]]
[[Category: Saccharolobus solfataricus]]
[[Category: Masullo, M]]
[[Category: Bocchini V]]
[[Category: Sica, F]]
[[Category: Masullo M]]
[[Category: Vitagliano, L]]
[[Category: Sica F]]
[[Category: Zagari, A]]
[[Category: Vitagliano L]]
[[Category: Alpha/beta structure]]
[[Category: Zagari A]]
[[Category: Gtpase]]
[[Category: Protein biosynthesis]]
[[Category: Translation]]

Latest revision as of 07:40, 7 February 2024

Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in complex with GDP

1jny, resolution 1.80Å

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