Structural study reveals the temperature-dependent conformational flexibility of Tk-PTP, a protein tyrosine phosphatase from Thermococcus kodakaraensis KOD1
Fig 7
Structural comparison with SsoPTP.
(A) Sequence alignment of Tk-PTP and SsoPTP. The secondary structure of Tk-PTP is shown together. Aligned residues are shaded green. The P-loop residues are presented in orange, and the GG motifs are highlighted by rectangles. (B) Structural alignment of Tk-PTP(form II) and SsoPTP in stereo views. Cα trace (top) and P-loop in sticks (bottom) of Tk-PTP(form II) are superimposed on those of SsoPTP. The P-loop and α4−α5 loop regions are indicated by dotted circles or rectangles, respectively (top). (C) The P-loop and α4−α5 loop regions of Tk-PTP(form II) are structurally compared to those of SsoPTP. Dotted circles highlight the guanidinium group of Arg127 of Tk-PTP(form II) or that of Arg130 of SsoPTP. Hydrogen bonds described in the main text are presented as dashed lines.