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| | <StructureSection load='5izl' size='340' side='right'caption='[[5izl]], [[Resolution|resolution]] 2.72Å' scene=''> | | <StructureSection load='5izl' size='340' side='right'caption='[[5izl]], [[Resolution|resolution]] 2.72Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5izl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IZL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IZL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5izl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IZL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.72Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5izk|5izk]], [[5izm|5izm]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EEFSEC, SELB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5izl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5izl OCA], [https://pdbe.org/5izl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5izl RCSB], [https://www.ebi.ac.uk/pdbsum/5izl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5izl 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=5izl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5izl OCA], [http://pdbe.org/5izl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5izl RCSB], [http://www.ebi.ac.uk/pdbsum/5izl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5izl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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. | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dobosz-Bartoszek, M]] | + | [[Category: Dobosz-Bartoszek M]] |
| - | [[Category: Simonovic, M]] | + | [[Category: Simonovic M]] |
| - | [[Category: Elongation factor]]
| + | |
| - | [[Category: Gdpcp]]
| + | |
| - | [[Category: Gtp]]
| + | |
| - | [[Category: Gtpase]]
| + | |
| - | [[Category: Selenocysteine]]
| + | |
| - | [[Category: Selenocysteine trna]]
| + | |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dobosz-Bartoszek M, Pinkerton MH, Otwinowski Z, Chakravarthy S, Soll D, Copeland PR, Simonovic M. Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation. Nat Commun. 2016 Oct 6;7:12941. doi: 10.1038/ncomms12941. PMID:27708257 doi:http://dx.doi.org/10.1038/ncomms12941
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