Structural study reveals the temperature-dependent conformational flexibility of Tk-PTP, a protein tyrosine phosphatase from Thermococcus kodakaraensis KOD1
Fig 4
Structural analysis of Tk-PTP(G95A).
(A) Stereo views of Cα trace of Tk-PTP(G95A) that are superimposed onto that of two forms of Tk-PTP. Dotted circles and rectangles indicate the P-loop and α4−α5 loop regions, respectively. (B) The P-loops of three Tk-PTP proteins are shown as labeled sticks and compared. Dashed lines represent hydrogen bonds and electrostatic interactions mediated by vanadate bound to Tk-PTP(form II) or by formate bound to Tk-PTP(G95A). (C) The P-loop and α4−α5 loop regions of Tk-PTP(G95A) are structurally aligned to those of the two forms of Tk-PTP.