7l1t
From Proteopedia
(Difference between revisions)
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<StructureSection load='7l1t' size='340' side='right'caption='[[7l1t]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='7l1t' size='340' side='right'caption='[[7l1t]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L1T FirstGlance]. <br> |
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</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]] 2.25Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7l1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l1t OCA], [https://pdbe.org/7l1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l1t RCSB], [https://www.ebi.ac.uk/pdbsum/7l1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l1t ProSAT]</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=7l1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l1t OCA], [https://pdbe.org/7l1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l1t RCSB], [https://www.ebi.ac.uk/pdbsum/7l1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l1t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/SPCS_HUMAN SPCS_HUMAN] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | O-Phosphoseryl-tRNASec selenium transferase (SepSecS) catalyzes the terminal step of selenocysteine (Sec) synthesis in archaea and eukaryotes. How the Sec synthetic machinery recognizes and discriminates tRNASec from the tRNA pool is essential to the integrity of the selenoproteome. Previously, we suggested that SepSecS adopts a competent conformation that is pre-ordered for catalysis. Herein, using high-resolution X-ray crystallography, we visualized tRNA-dependent conformational changes in human SepSecS that may be a prerequisite for achieving catalytic competency. We show that tRNASec binding organizes the active sites of the catalytic protomer, while stabilizing the N- and C-termini of the non-catalytic protomer. Binding of large anions to the catalytic groove may further optimize the catalytic site for substrate binding and catalysis. Our biochemical and mutational analyses demonstrate that productive SepSecS*tRNASec complex formation is enthalpically driven and primarily governed by electrostatic interactions between the acceptor-, TPsiC-, and variable arms of tRNASec and helices alpha1 and alpha14 of SepSecS. The detailed visualization of the tRNA-dependent activation of SepSecS provides a structural basis for a revised model of the terminal reaction of Sec formation in archaea and eukaryotes. | ||
| - | |||
| - | Structural basis for the tRNA-dependent activation of the terminal complex of selenocysteine synthesis in humans.,Puppala AK, Castillo Suchkou J, French RL, Kiernan KA, Simonovic M Nucleic Acids Res. 2023 Mar 17:gkad182. doi: 10.1093/nar/gkad182. PMID:36929010<ref>PMID:36929010</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 7l1t" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Selenocysteine synthase|Selenocysteine synthase]] | *[[Selenocysteine synthase|Selenocysteine synthase]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Castillo Suchkou J]] | [[Category: Castillo Suchkou J]] | ||
[[Category: Puppala A]] | [[Category: Puppala A]] | ||
[[Category: Simonovic M]] | [[Category: Simonovic M]] | ||
Current revision
Crystal structure of human holo SepSecS
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