View source for 6iht


==Crystal structure of bacterial serine phosphatase bound with phosphorylated peptide==
<StructureSection load='6iht' size='340' side='right'caption='[[6iht]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6iht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Peptide_display_vector_fth1 Peptide display vector fth1] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IHT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.569&#8491;</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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=6iht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iht OCA], [https://pdbe.org/6iht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iht RCSB], [https://www.ebi.ac.uk/pdbsum/6iht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iht ProSAT]</span></td></tr>
</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iht" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Peptide display vector fth1]]
[[Category: Staphylococcus aureus]]
[[Category: Yang C-G]]
[[Category: Yang T]]