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| | ==Crystal structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus== | | ==Crystal structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus== |
| - | <StructureSection load='2zau' size='340' side='right' caption='[[2zau]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2zau' size='340' side='right'caption='[[2zau]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zau]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZAU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zau]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZAU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zod|2zod]], [[2yye|2yye]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">selD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 "Aquifex aeolicus" Huber and Stetter 2001])</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=2zau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zau OCA], [https://pdbe.org/2zau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zau RCSB], [https://www.ebi.ac.uk/pdbsum/2zau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zau ProSAT], [https://www.topsan.org/Proteins/RSGI/2zau TOPSAN]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Selenide,_water_dikinase Selenide, water dikinase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zau OCA], [http://pdbe.org/2zau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zau RCSB], [http://www.ebi.ac.uk/pdbsum/2zau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zau ProSAT], [http://www.topsan.org/Proteins/RSGI/2zau TOPSAN]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SELD_AQUAE SELD_AQUAE]] Synthesizes selenophosphate from selenide and ATP (By similarity). | + | [https://www.uniprot.org/uniprot/SELD_AQUAE SELD_AQUAE] Synthesizes selenophosphate from selenide and ATP (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zau_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zau_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquifex aeolicus huber and stetter 2001]] | + | [[Category: Aquifex aeolicus]] |
| - | [[Category: Selenide, water dikinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Matsumoto, E]] | + | [[Category: Matsumoto E]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Sekine S]] |
| - | [[Category: Sekine, S]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Intramolecular s-s bond]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Magnesium]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Selenium]]
| + | |
| - | [[Category: Selenocysteine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Trimer of dimer]]
| + | |
| Structural highlights
Function
SELD_AQUAE Synthesizes selenophosphate from selenide and ATP (By similarity).
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 (SPS) catalyzes the activation of selenide with ATP to synthesize selenophosphate, the reactive selenium donor for biosyntheses of both the 21st amino acid selenocysteine and 2-selenouridine nucleotides in tRNA anticodons. The crystal structure of an N-terminally (25 residues) truncated fragment of SPS (SPS-DeltaN) from Aquifex aeolicus has been determined at 2.0 A resolution. The structure revealed SPS to be a two-domain alpha/beta protein, with domain folds that are homologous to those of PurM-superfamily proteins. In the crystal, six monomers of SPS-DeltaN form a hexamer of 204 kDa, whereas the molecular weight estimated by ultracentrifugation was approximately 63 kDa, which is comparable to the calculated weight of the dimer (68 kDa).
Structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus.,Matsumoto E, Sekine SI, Akasaka R, Otta Y, Katsura K, Inoue M, Kaminishi T, Terada T, Shirouzu M, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):453-8. Epub 2008 May 16. PMID:18540050[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsumoto E, Sekine SI, Akasaka R, Otta Y, Katsura K, Inoue M, Kaminishi T, Terada T, Shirouzu M, Yokoyama S. Structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):453-8. Epub 2008 May 16. PMID:18540050 doi:http://dx.doi.org/10.1107/S1744309108012074
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