Crystallization (Comment) | Organism |
---|---|
isozyme PtpA with a peptide bound in the active site mimicking a phosphotyrosine substrate, X-ray diffraction structure determination and analysis at 1.0 A resolution | Staphylococcus aureus |
Protein Variants | Comment | Organism |
---|---|---|
D120A | site-directed mutagenesis, the mutation abrogates activity of PtpA with the artificial phosphatase substrate 4-nitrophenol phosphate, confirming its essentiality for function | Staphylococcus aureus |
additional information | genetic deletion of ptpA or ptpB does not affect in vitro growth or cell wall integrity | Staphylococcus aureus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | inhibitor design using the crystal structure of PtpA, overview | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
two low-molecular-weight protein tyrosine phosphatases, PtpA and PtpB | - |
Subunits | Comment | Organism |
---|---|---|
More | PtpA adopts a single domain, alpha/beta fold with a central four-stranded parallel beta-sheet providing the scaffold for the active site, analysis of the PtpA structural relations within the PTP family, and sequence comparison with the human isozymes, overview | Staphylococcus aureus |
Synonyms | Comment | Organism |
---|---|---|
protein tyrosine phosphatase | - |
Staphylococcus aureus |
PtpA | - |
Staphylococcus aureus |
PtpB | - |
Staphylococcus aureus |
General Information | Comment | Organism |
---|---|---|
additional information | Asp120 has an essentiality function as the general acid. Two adjacent tyrosine residues, Tyr122 and Tyr123, contribute to the deepening of the active-site pocket. Genetic deletion of ptpA or ptpB does not affect in vitro growth or cell wall integrity | Staphylococcus aureus |
physiological function | PtpA is not essential for in vitro growth | Staphylococcus aureus |