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| | <StructureSection load='6ihs' size='340' side='right'caption='[[6ihs]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='6ihs' size='340' side='right'caption='[[6ihs]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ihs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IHS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ihs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IHS 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></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]] 1.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prpC, BN1321_240063, BTN44_06615, CSC83_01010, CSC87_08725, EP54_08495, EQ90_08165, ERS072840_01404, RK64_06500 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=6ihs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ihs OCA], [https://pdbe.org/6ihs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ihs RCSB], [https://www.ebi.ac.uk/pdbsum/6ihs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ihs 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=6ihs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ihs OCA], [http://pdbe.org/6ihs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ihs RCSB], [http://www.ebi.ac.uk/pdbsum/6ihs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ihs ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9RL81_STAAU Q9RL81_STAAU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphoprotein phosphatase]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Yang, C G]] | + | [[Category: Yang C-G]] |
| - | [[Category: Yang, T]] | + | [[Category: Yang T]] |
| - | [[Category: Bacteria]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metal binding]]
| + | |
| - | [[Category: Phosphatase]]
| + | |
| Structural highlights
Function
Q9RL81_STAAU
Publication Abstract from PubMed
Staphylococcus aureus Stp1, which belongs to the bacterial metal-dependent protein phosphatase (PPM) family, is a promising candidate for antivirulence targeting. How Stp1 recognizes the phosphorylated peptide remains unclear, however. In order to investigate the recognition mechanism of Stp1 in depth, we have determined a series of crystal structures of S. aureus Stp1 in different states and the structural complex of Stp1 bound with a phosphorylated peptide His12. Different phosphorylated peptides, including MgrA- and GraR-derived phosphopeptides, are substrates of Stp1, which supports the function of Stp1 as a selective Ser/Thr phosphatase. In addition, interestingly, the crystal structures of R161-Stp1 variants combined with the biochemical activity validations have uncovered that R161 residue plays a key role to control the conformation switches of the flap domain in order to facilitate substrate binding and the dephosphorylation process. Our findings provide crucial structural insight into the molecular mechanism of S. aureus Stp1 phosphatase and reveal the phosphorylated peptides for biochemistry study and inhibitor screening of Stp1.
Structural Insight into the Mechanism of Staphylococcus aureus Stp1 Phosphatase.,Yang T, Liu T, Gan J, Yu K, Chen K, Xue W, Lan L, Yang S, Yang CG ACS Infect Dis. 2019 Jun 14;5(6):841-850. doi: 10.1021/acsinfecdis.8b00316. Epub , 2019 Mar 25. PMID:30868877[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang T, Liu T, Gan J, Yu K, Chen K, Xue W, Lan L, Yang S, Yang CG. Structural Insight into the Mechanism of Staphylococcus aureus Stp1 Phosphatase. ACS Infect Dis. 2019 Jun 14;5(6):841-850. doi: 10.1021/acsinfecdis.8b00316. Epub , 2019 Mar 25. PMID:30868877 doi:http://dx.doi.org/10.1021/acsinfecdis.8b00316
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