5izm: Difference between revisions

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'''Unreleased structure'''


The entry 5izm is ON HOLD  until Paper Publication
==The crystal structure of human eEFSec in complex with GDPNP==
<StructureSection load='5izm' size='340' side='right' caption='[[5izm]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5izm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IZM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5izl|5izl]], [[5izk|5izk]]</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=5izm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5izm OCA], [http://pdbe.org/5izm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5izm RCSB], [http://www.ebi.ac.uk/pdbsum/5izm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5izm ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SELB_HUMAN SELB_HUMAN]] Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Selenocysteine is the only proteinogenic amino acid encoded by a recoded in-frame UGA codon that does not operate as the canonical opal stop codon. A specialized translation elongation factor, eEFSec in eukaryotes and SelB in prokaryotes, promotes selenocysteine incorporation into selenoproteins by a still poorly understood mechanism. Our structural and biochemical results reveal that four domains of human eEFSec fold into a chalice-like structure that has similar binding affinities for GDP, GTP and other guanine nucleotides. Surprisingly, unlike in eEF1A and EF-Tu, the guanine nucleotide exchange does not cause a major conformational change in domain 1 of eEFSec, but instead induces a swing of domain 4. We propose that eEFSec employs a non-canonical mechanism involving the distinct C-terminal domain 4 for the release of the selenocysteinyl-tRNA during decoding on the ribosome.


Authors:  
Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.,Dobosz-Bartoszek M, Pinkerton MH, Otwinowski Z, Chakravarthy S, Soll D, Copeland PR, Simonovic M Nat Commun. 2016 Oct 6;7:12941. doi: 10.1038/ncomms12941. PMID:27708257<ref>PMID:27708257</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5izm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dobosz-Bartoszek, M]]
[[Category: Otwinowski, Z]]
[[Category: Simonovic, M]]
[[Category: Elongation factor]]
[[Category: Gdpnp]]
[[Category: Gtp]]
[[Category: Gtpase]]
[[Category: Selenocysteine]]
[[Category: Selenocysteine trna]]
[[Category: Translation]]