3wya: Difference between revisions

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==Crystal structure of GDP-bound EF1alpha from Pyrococcus horikoshii==
==Crystal structure of GDP-bound EF1alpha from Pyrococcus horikoshii==
<StructureSection load='3wya' size='340' side='right' caption='[[3wya]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='3wya' size='340' side='right'caption='[[3wya]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3wya]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WYA FirstGlance]. <br>
<table><tr><td colspan='2'>[[3wya]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WYA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.35&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wy9|3wy9]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wya OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wya RCSB], [http://www.ebi.ac.uk/pdbsum/3wya PDBsum]</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=3wya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wya OCA], [https://pdbe.org/3wya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wya RCSB], [https://www.ebi.ac.uk/pdbsum/3wya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wya ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EF1A_PYRHO EF1A_PYRHO]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]  
[https://www.uniprot.org/uniprot/EF1A_PYRHO EF1A_PYRHO] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3wya" style="background-color:#fffaf0;"></div>
==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Honda, T]]
[[Category: Large Structures]]
[[Category: Ito, K]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Miyoshi, T]]
[[Category: Honda T]]
[[Category: Murakami, R]]
[[Category: Ito K]]
[[Category: Suzuki, T]]
[[Category: Miyoshi T]]
[[Category: Uchiumi, T]]
[[Category: Murakami R]]
[[Category: Yao, M]]
[[Category: Suzuki T]]
[[Category: Aminoacyl-trna delivery]]
[[Category: Uchiumi T]]
[[Category: Gtp]]
[[Category: Yao M]]
[[Category: Gtpase]]
[[Category: Multi-domain]]
[[Category: Stalk protein]]
[[Category: Translation]]

Latest revision as of 22:22, 29 May 2024

Crystal structure of GDP-bound EF1alpha from Pyrococcus horikoshiiCrystal structure of GDP-bound EF1alpha from Pyrococcus horikoshii

Structural highlights

3wya is a 1 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.35Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EF1A_PYRHO This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118]

Publication Abstract from PubMed

In all organisms, the large ribosomal subunit contains multiple copies of a flexible protein, the so-called 'stalk'. The C-terminal domain (CTD) of the stalk interacts directly with the translational GTPase factors, and this interaction is required for factor-dependent activity on the ribosome. Here we have determined the structure of a complex of the CTD of the archaeal stalk protein aP1 and the GDP-bound archaeal elongation factor aEF1alpha at 2.3 A resolution. The structure showed that the CTD of aP1 formed a long extended alpha-helix, which bound to a cleft between domains 1 and 3 of aEF1alpha, and bridged these domains. This binding between the CTD of aP1 and the aEF1alpha*GDP complex was formed mainly by hydrophobic interactions. The docking analysis showed that the CTD of aP1 can bind to aEF1alpha*GDP located on the ribosome. An additional biochemical assay demonstrated that the CTD of aP1 also bound to the aEF1alpha*GTP*aminoacyl-tRNA complex. These results suggest that the CTD of aP1 interacts with aEF1alpha at various stages in translation. Furthermore, phylogenetic perspectives and functional analyses suggested that the eukaryotic stalk protein also interacts directly with domains 1 and 3 of eEF1alpha, in a manner similar to the interaction of archaeal aP1 with aEF1alpha.

Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1alpha.,Ito K, Honda T, Suzuki T, Miyoshi T, Murakami R, Yao M, Uchiumi T Nucleic Acids Res. 2014 Dec 16;42(22):14042-52. doi: 10.1093/nar/gku1248. Epub, 2014 Nov 26. PMID:25428348[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Ito K, Honda T, Suzuki T, Miyoshi T, Murakami R, Yao M, Uchiumi T. Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1alpha. Nucleic Acids Res. 2014 Dec 16;42(22):14042-52. doi: 10.1093/nar/gku1248. Epub, 2014 Nov 26. PMID:25428348 doi:http://dx.doi.org/10.1093/nar/gku1248

3wya, resolution 2.35Å

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