5izk
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of human eEFSec in complex with GDP== |
| + | <StructureSection load='5izk' size='340' side='right' caption='[[5izk]], [[Resolution|resolution]] 3.25Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5izk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IZK 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> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5izm|5izm]], [[5izl|5izl]]</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=5izk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5izk OCA], [http://pdbe.org/5izk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5izk RCSB], [http://www.ebi.ac.uk/pdbsum/5izk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5izk 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5izk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Dobosz-Bartoszek, M]] | ||
| + | [[Category: Simonovic, M]] | ||
| + | [[Category: Elongation factor]] | ||
| + | [[Category: Gdp]] | ||
| + | [[Category: Gtpase]] | ||
| + | [[Category: Selenocysteine]] | ||
| + | [[Category: Selenocysteine trna]] | ||
| + | [[Category: Translation]] | ||
Revision as of 09:30, 19 October 2016
The crystal structure of human eEFSec in complex with GDP
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