scholarly journals The SPOT technique as a tool for studying protein tyrosine phosphatase substrate specificities

2009 ◽  
Vol 11 (10) ◽  
pp. 2326-2334 ◽  
Author(s):  
Xavier Espanel ◽  
Martine Huguenin-Reggiani ◽  
Rob Hooft van Huijsduijnen
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Substrate Specificities ◽  
Protein Tyrosine ◽  
Phosphatase Substrate

scholarly journals Crystal Structure of Low-Molecular-Weight Protein Tyrosine Phosphatase from Mycobacterium tuberculosis at 1.9-Å Resolution

2005 ◽  
Vol 187 (6) ◽  
pp. 2175-2181 ◽  
Author(s):  
Chaithanya Madhurantakam ◽  
Eerappa Rajakumara ◽  
Pooja Anjali Mazumdar ◽  
Baisakhee Saha ◽  
Devrani Mitra ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Active Site ◽  
Tyrosine Phosphatase ◽  
Chloride Ion ◽  
Low Molecular Weight ◽  
Molecular Weight Protein ◽  
Substrate Specificities ◽  
Protein Tyrosine ◽  
Weight Protein ◽  
Low Molecular Weight Protein

ABSTRACT The low-molecular-weight protein tyrosine phosphatase (LMWPTPase) belongs to a distinctive class of phosphotyrosine phosphatases widely distributed among prokaryotes and eukaryotes. We report here the crystal structure of LMWPTPase of microbial origin, the first of its kind from Mycobacterium tuberculosis. The structure was determined to be two crystal forms at 1.9- and 2.5-Å resolutions. These structural forms are compared with those of the LMWPTPases of eukaryotes. Though the overall structure resembles that of the eukaryotic LMWPTPases, there are significant changes around the active site and the protein tyrosine phosphatase (PTP) loop. The variable loop forming the wall of the crevice leading to the active site is conformationally unchanged from that of mammalian LMWPTPase; however, differences are observed in the residues involved, suggesting that they have a role in influencing different substrate specificities. The single amino acid substitution (Leu12Thr [underlined below]) in the consensus sequence of the PTP loop, C T GNICRS, has a major role in the stabilization of the PTP loop, unlike what occurs in mammalian LMWPTPases. A chloride ion and a glycerol molecule were modeled in the active site where the chloride ion interacts in a manner similar to that of phosphate with the main chain nitrogens of the PTP loop. This structural study, in addition to identifying specific mycobacterial features, may also form the basis for exploring the mechanism of the substrate specificities of bacterial LMWPTPases.

scholarly journals Probing Protein-tyrosine Phosphatase Substrate Specificity Using a Phosphotyrosine-containing Phage Library

2003 ◽  
Vol 279 (1) ◽  
pp. 311-318 ◽  
Author(s):  
Sébastien Wälchli ◽  
Xavier Espanel ◽  
Axel Harrenga ◽  
Mario Rossi ◽  
Gianni Cesareni ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Phage Library ◽  
Protein Tyrosine ◽  
Phosphatase Substrate

Phospho-azatyrosine, a less effective protein-tyrosine phosphatase substrate than phosphotyrosine

2001 ◽  
Vol 11 (10) ◽  
pp. 1265-1268
Author(s):  
Terrence R Burke ◽  
Zhu-Jun Yao ◽  
Bin Ye ◽  
Kengo Miyoshi ◽  
Akira Otaka ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Phosphatase Substrate
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