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PDBsum entry 6ihu
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PDB id:
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Hydrolase
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Title:
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Crystal structure of bacterial serine phosphatase bearing r161a mutation
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Structure:
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Phosphorylated protein phosphatase. Chain: a. Synonym: protein phosphatase,protein serine/threonine phosphatase prpc,regulation of stationary phase,protein-serine/threonine phosphatase stp1,serine/threonine-protein phosphatase. Engineered: yes. Mutation: yes
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Source:
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Staphylococcus aureus. Organism_taxid: 1280. Gene: prpc, prpc_1, bn1321_240063, btn44_06615, csc83_01010, csc87_08725, ep54_08495, eq90_08165, ers072840_01404, nctc11940_01141, nctc13131_00423, nctc13196_02843, nctc9944_01222, rk64_06500, samea1469870_01594, samea1531701_01402. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.84Å
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R-factor:
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0.171
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R-free:
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0.200
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Authors:
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C.-G.Yang,T.Yang
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Key ref:
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T.Yang
et al.
(2019).
Structural Insight into the Mechanism of Staphylococcus aureus Stp1 Phosphatase.
ACS Infect Dis,
5,
841-850.
PubMed id:
DOI:
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Date:
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02-Oct-18
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Release date:
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07-Aug-19
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PROCHECK
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Headers
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References
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Q9RL81
(Q9RL81_STAAU) -
Phosphorylated protein phosphatase from Staphylococcus aureus
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Seq:
Struc:
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247 a.a.
220 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Enzyme class:
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E.C.3.1.3.16
- protein-serine/threonine phosphatase.
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Reaction:
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1.
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O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
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2.
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O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
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O-phospho-L-seryl-[protein]
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+
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H2O
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=
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L-seryl-[protein]
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+
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phosphate
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O-phospho-L-threonyl-[protein]
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+
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H2O
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=
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L-threonyl-[protein]
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+
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phosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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ACS Infect Dis
5:841-850
(2019)
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PubMed id:
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Structural Insight into the Mechanism of Staphylococcus aureus Stp1 Phosphatase.
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T.Yang,
T.Liu,
J.Gan,
K.Yu,
K.Chen,
W.Xue,
L.Lan,
S.Yang,
C.G.Yang.
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ABSTRACT
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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.
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Links
