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<StructureSection load='6ihv' size='340' side='right'caption='[[6ihv]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6ihv' size='340' side='right'caption='[[6ihv]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6ihv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IHV OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6ihv]] 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=6IHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IHV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ihv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ihv OCA], [https://pdbe.org/6ihv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ihv RCSB], [https://www.ebi.ac.uk/pdbsum/6ihv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ihv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9RL81_STAAU Q9RL81_STAAU] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:30868877</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ihv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Staphylococcus aureus]] | ||
[[Category: Yang | [[Category: Yang C-G]] | ||
[[Category: Yang | [[Category: Yang T]] | ||
Latest revision as of 12:41, 22 November 2023
Crystal structure of bacterial serine phosphatase bearing R161E mutationCrystal structure of bacterial serine phosphatase bearing R161E mutation
Structural highlights
FunctionPublication Abstract from PubMedStaphylococcus 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
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