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| | <StructureSection load='3fd6' size='340' side='right'caption='[[3fd6]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='3fd6' size='340' side='right'caption='[[3fd6]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fd6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FD6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fd6]] 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=3FD6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FD6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.95Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2yye|2yye]], [[3fd5|3fd5]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEPHS1, SELD, SPS, SPS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Selenide,_water_dikinase Selenide, water dikinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.9.3 2.7.9.3] </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=3fd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fd6 OCA], [https://pdbe.org/3fd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fd6 RCSB], [https://www.ebi.ac.uk/pdbsum/3fd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fd6 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=3fd6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fd6 OCA], [https://pdbe.org/3fd6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fd6 RCSB], [https://www.ebi.ac.uk/pdbsum/3fd6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fd6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SPS1_HUMAN SPS1_HUMAN]] Synthesizes selenophosphate from selenide and ATP.<ref>PMID:7665581</ref>
| + | [https://www.uniprot.org/uniprot/SPS1_HUMAN SPS1_HUMAN] Synthesizes selenophosphate from selenide and ATP.<ref>PMID:7665581</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Selenide, water dikinase]]
| + | [[Category: Wang KT]] |
| - | [[Category: Wang, K T]] | + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Seld]]
| + | |
| - | [[Category: Selenium]]
| + | |
| - | [[Category: Selenophosphate synthetase 1]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
SPS1_HUMAN Synthesizes selenophosphate from selenide and ATP.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Selenophosphate synthetase catalyzes the synthesis of the highly active selenium donor molecule selenophosphate, a key intermediate in selenium metabolism. We have determined the high-resolution crystal structure of human selenophosphate synthetase 1 (hSPS1). An unexpected reaction intermediate, with a tightly bound phosphate and ADP at the active site has been captured in the structure. An enzymatic assay revealed that hSPS1 possesses low ADP hydrolysis activity in the presence of phosphate. Our structural and enzymatic results suggest that consuming the second high-energy phosphoester bond of ATP could protect the labile product selenophosphate during catalytic reaction. We solved another hSPS1 structure with potassium ions at the active sites. Comparing the two structures, we were able to define the monovalent cation-binding site of the enzyme. The detailed mechanism of the ADP hydrolysis step and the exact function of the monovalent cation for hSPS1 catalytic reaction are proposed.
Crystal structures of catalytic intermediates of human selenophosphate synthetase 1.,Wang KT, Wang J, Li LF, Su XD J Mol Biol. 2009 Jul 24;390(4):747-59. Epub 2009 May 25. PMID:19477186[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Low SC, Harney JW, Berry MJ. Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis. J Biol Chem. 1995 Sep 15;270(37):21659-64. PMID:7665581
- ↑ Wang KT, Wang J, Li LF, Su XD. Crystal structures of catalytic intermediates of human selenophosphate synthetase 1. J Mol Biol. 2009 Jul 24;390(4):747-59. Epub 2009 May 25. PMID:19477186 doi:10.1016/j.jmb.2009.05.032
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