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| | <StructureSection load='4o8c' size='340' side='right'caption='[[4o8c]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4o8c' size='340' side='right'caption='[[4o8c]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o8c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O8C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o8c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O8C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kn8|4kn8]]</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=4o8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o8c OCA], [https://pdbe.org/4o8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o8c RCSB], [https://www.ebi.ac.uk/pdbsum/4o8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o8c ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] </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=4o8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o8c OCA], [http://pdbe.org/4o8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o8c RCSB], [http://www.ebi.ac.uk/pdbsum/4o8c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o8c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8L1N9_GEOSE Q8L1N9_GEOSE] |
| | <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: Alkaline phosphatase]] | + | [[Category: Geobacillus stearothermophilus]] |
| - | [[Category: Atcc 12980]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gong, W]] | + | [[Category: Gong W]] |
| - | [[Category: Guo, Z]] | + | [[Category: Guo Z]] |
| - | [[Category: Ji, C]] | + | [[Category: Ji C]] |
| - | [[Category: Shen, T]] | + | [[Category: Shen T]] |
| - | [[Category: Wang, F]] | + | [[Category: Wang F]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| Structural highlights
Function
Q8L1N9_GEOSE
Publication Abstract from PubMed
Using directed evolution based on random mutagenesis and heat-treated selection, a thermostable His170Tyr mutant of Geobacillus stearothermophilus thermostable p-nitrophenylphosphatase (TpNPPase) was obtained. The temperature at which the His170Tyr mutant lost 50% of its activity (T1/2) was found to be 4.40 K higher than that of wild-type TpNPPase, and the melting temperature of the His170Tyr mutant increased by 2.39 K. The crystal structure of the His170Tyr mutant was then determined at 2.0 A resolution in the presence of a sodium ion and a sulfate ion in the active site. The cap domain of chain B shows a half-closed conformation. The hydrophobic side chain of the mutated residue, the hydroxyphenyl group, forms a hydrophobic contact with the methyl group of Ala166. This hydrophobic interaction was found using the Protein Interactions Calculator (PIC) web server with an interaction distance of 4.6 A, and might be a key factor in the thermostabilization of the His170Tyr mutant. This study potentially offers a molecular basis for both investigation of the catalytic mechanism and thermostable protein engineering.
Structure of a His170Tyr mutant of thermostable pNPPase from Geobacillus stearothermophilus.,Shen T, Guo Z, Ji C Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):697-702. doi:, 10.1107/S2053230X14007341. Epub 2014 May 10. PMID:24915075[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shen T, Guo Z, Ji C. Structure of a His170Tyr mutant of thermostable pNPPase from Geobacillus stearothermophilus. Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):697-702. doi:, 10.1107/S2053230X14007341. Epub 2014 May 10. PMID:24915075 doi:http://dx.doi.org/10.1107/S2053230X14007341
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