Structural study reveals the temperature-dependent conformational flexibility of Tk-PTP, a protein tyrosine phosphatase from Thermococcus kodakaraensis KOD1
Fig 6
Characterization of thermostability of Tk-PTP.
(A) Melting points of three different constructs of Tk-PTP and four PTP proteins. All the measurements were carried out twice. (B) Number of intramolecular carbon−carbon contacts within 4.5 Å mediated by side chain atoms of Tk-PTP and three human DUSP proteins are analyzed and compared. “Hydrophilic functional group” includes imidazole of histidine, guanidinium of arginine, carboxylates of aspartate or glutamate, and amides of asparagine or glutamine. (C) Intramolecular interactions within Tk-PTP(form II) and DUSP3. The three hydrophobic residues of Tk-PTP that were substituted in A and the corresponding residues of DUSP3 are marked in red.