This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4c0s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (17:19, 7 September 2022) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='4c0s' size='340' side='right'caption='[[4c0s]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='4c0s' size='340' side='right'caption='[[4c0s]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4c0s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0S FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4c0s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0S 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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+
</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4c0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0s OCA], [https://pdbe.org/4c0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0s RCSB], [https://www.ebi.ac.uk/pdbsum/4c0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0s ProSAT]</span></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=4c0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0s OCA], [http://pdbe.org/4c0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0s RCSB], [http://www.ebi.ac.uk/pdbsum/4c0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0s ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[[https://www.uniprot.org/uniprot/EF1A2_RABIT EF1A2_RABIT]]
-
Eukaryotic elongation factor eEF1A transits between the GTP- and GDP-bound conformations during the ribosomal polypeptide chain elongation. eEF1A*GTP establishes a complex with the aminoacyl-tRNA in the A site of the 80S ribosome. Correct codon-anticodon recognition triggers GTP hydrolysis, with subsequent dissociation of eEF1A*GDP from the ribosome. The structures of both the 'GTP'- and 'GDP'-bound conformations of eEF1A are unknown. Thus, the eEF1A-related ribosomal mechanisms were anticipated only by analogy with the bacterial homolog EF-Tu. Here, we report the first crystal structure of the mammalian eEF1A2*GDP complex which indicates major differences in the organization of the nucleotide-binding domain and intramolecular movements of eEF1A compared to EF-Tu. Our results explain the nucleotide exchange mechanism in the mammalian eEF1A and suggest that the first step of eEF1A*GDP dissociation from the 80S ribosome is the rotation of the nucleotide-binding domain observed after GTP hydrolysis.
+
-
 
+
-
Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.,Crepin T, Shalak VF, Yaremchuk AD, Vlasenko DO, McCarthy A, Negrutskii BS, Tukalo MA, El'skaya AV Nucleic Acids Res. 2014 Oct 17. pii: gku974. PMID:25326326<ref>PMID:25326326</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4c0s" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
-
*[[Elongation factor|Elongation factor]]
+
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
-
[[Category: Crepin, T]]
+
[[Category: Crepin T]]
-
[[Category: McCarthy, A A]]
+
[[Category: El'skaya AV]]
-
[[Category: Negrutskii, B S]]
+
[[Category: McCarthy AA]]
-
[[Category: Shalak, V F]]
+
[[Category: Negrutskii BS]]
-
[[Category: Tukalo, M A]]
+
[[Category: Shalak VF]]
-
[[Category: Vlasenko, D O]]
+
[[Category: Tukalo MA]]
-
[[Category: Yaremchuk, A D]]
+
[[Category: Vlasenko DO]]
-
[[Category: Skaya, A V.El]]
+
[[Category: Yaremchuk AD]]
-
[[Category: Translation]]
+

Current revision

Mammalian translation elongation factor eEF1A2

PDB ID 4c0s

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4c0s"
Personal tools