Yersinia phosphatase

Table 2. Predicted intrinsic and apparent pKa values for the Cys403 residue in Yersinia phosphatase for different models of the structure the data refer to a temperature of 293 K and an ionic strength corresponding to 150 mM of monovalent salt. See the text for the detailed description of the conditions under which each pK estimation was made. The experimentally determined value is 4.67 [39]...

Miao et al. (2003) have been able to reconstitute the essential features of retraction in vitro by adding Yersinia phosphatase (YOP) to the MSP-based motility apparatus assembled from cell-free extracts from Ascaris sperm... 

Fig. 5. Retraction requires Yersinia phosphatase (YOP) plus an additional component in S-100. (A) Time-lapse sequence of phase contrast micrographs of a fiber assembled in S-100 and then perfused with S-100 containing YOP. The vesicle-bearing end of the fiber is at the top. With time, the fiber shortened and its optical density decreased. Numbers in each frame are elapsed time in minutes. (B) Fiber perfused with YOP in KPM assembly buffer. Without S-100 present, the fiber lost optical density but exhibited very litde shortening. (C) A similar sequence showing a fiber perfused with S-100 containing 1 mM ATP, but without added YOP. The fiber continued to grow at its vesicle bearing end and did not retract. Bars, 5 /im. Reproduced from Science, 2003, vol. 302, pp. 1405-1407.

Zhang, Z.-Y., Dixon, J. E. Active site labeling of the yersinia protein tyrosine phosphatase The determination of the pKa of active site cysteine and the function of the conserved histidine 402. Biochem. 32 (1993) 9340-9345. 

Stuckey, I-A., Schubert, H.L., Baumann, E.B., Zhang, Z., Dixon, IE. and Saper, M.A. Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate (1994) Nature 370, 571-575... 

Hu, X., Stebbins, C. E. Molecular Docking and 3D QSAR Studies of Yersinia Protein Tyrosine Phosphatase YopH Inhibitors. Bioorg. Med. Chem. 2005, 13, 1101-1109. 

The best-studied protein tyrosine phosphatases are the high molecular weight cytoplasmic enzymes of the FTP family. X-ray structures of the human FTP IB cytosolic tyrosine phosphatase, have been solved by David Barford et and that of a Yersinia tyrosine phosphatase by Fauman et In Fig. 3.9a and b the structures of the... 

E. B. Fauman, Ch. Yuvaniyama, H. L. Schubert, ]. A. Stuckey, and M. A. Saper. The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications. JBwlChem, 111, 18780-18788, 1996. 

Hu X, Stebbins CE. Molecular docking and 3D-QSAR studies of Yersinia protein tyrosine phosphatase YopH inhibitors. Bioorg. Med. Chem. 2005 13 1101-1109. 

The X-ray structures of a number of PTPases have been reported, including the catalytic domains of PTP1B complexed with tungstate150 and of Yop51 from Yersinia (residues 163-468)151 with and without complexed tungstate. The structure of the human dual-specific phosphatase VHR (Vaccina HI-related) has also been determined,152 as well as those of several low-molecular-weight PTPases, including... 

KIEs and pH-rate dependencies for V/K were measured for the reactions of the dual-specificity phosphatase VHR177 and the Yersinia PTP178 with the alkyl phosphate mNBP, which, with a leaving group pK l of 14.9, is a better mimic for physiological alkyl phosphate substrates like phosphoserine or phosphothreonine. In... 

Keng YF, Wu L, Zhang ZY (1999) Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase. Eur J Biochem 259 809-814... 

Hoff RH, Hengge AC, Wu L et al (2000) Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia. Biochemistry 39 46-54... 

Tautz L, Bruckner S, Sareth S et al (2005) Inhibition of Yersinia tyrosine phosphatase by furanyl salicylate compounds. J Biol Chem 280 9400-9408... 

The PTPs catalyze the hydrolysis of phosphorylated tyrosine residues in proteins, to yield the free tyrosine side chains and inorganic phosphate. They are classified according to substrate specificity (1) tyrosine-specific PTPs, such as the Yersinia PTP (YopH) and the mammalian PTPIB and PTPl, which in vivo hydrolyze only pTyr residues as well as (2) the dual-specificity phosphatases (DSPs), such as the human VHR and Cdc25, which hydrolyze pTyr and pSer and pThr residues of protein substrates. Based on their cellular localization, PTPs are classified as receptor-like or intracellular. ... 

Guan K, Dixon JE. Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science. 1990 249 553-556. 

Fig. 9. Active site residues of PTPs, using the residue numbering from the PTP YopH from Yersinia. The catalytic residues are conserved among all PTPs, including the low molecular weight and the dual-specificity phosphatases.

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