Structural study reveals the temperature-dependent conformational flexibility of Tk-PTP, a protein tyrosine phosphatase from Thermococcus kodakaraensis KOD1
Fig 3
Structural comparison between two forms of Tk-PTP.
Stereo views of two forms of Tk-PTP for structural comparison. Dotted circles indicate the backbone carbonyl of Val131 undergoing a peptide flip. Hydrogen bonds described in the main text are presented as dashed lines. (A) The P-loop and α4−α5 loop of two forms of Tk-PTP are structurally compared. The GG motif residues are labeled in blue, while Arg124 and Arg127 are labeled in red. (B) The conformation of dual general acid/base residues (labeled in red) are structurally compared between two forms of Tk-PTP.