Figure 1 - full size


Figure 1.
Figure 1. (a) A ribbon diagram of the SSH2-C. Secondary structural elements (helix, orange; strand, blue; loop, grey), which were assigned with the program PROCHECK,[16] are labeled. Catalytic triads (D377, C392S, and R398) and bound sulfate ion are shown as a ball-and-stick representation. Boundaries of secondary structural elements are 1 (309-312), 2(315-318), 3(334-339), 4(353-356), 5(387-391), 1(320-323), 2(326-331), 3(371-383), 4(398-411), 5(415-425), and 6(433-447). (b) The superpositions of seven DSP structures representing each subfamily. A C trace of the DSP18 is superposed with that of VHR. Worm model is in blue for SSH2-C, orange for MKP-3 (pdb code:1mkp), green for VHR (pdb code:1vhr), cyan for PRL-1 (pdb code:1xm2), yellow for CDC14B (pdb code:1ohe), red for PTEN (pdb code:1d5r), and magenta for myotubularin2 (pdb code:1m7r), respectively. The superposition statistics against SSH2-C is 1.5/142 for MKP-3, 1.3/143 for VHR, 1.7/121 for PRL-1, 1.6/121 for CDC14B, 1.6/124 for PTEN, and 2.2/113 for Myotubularin2 where the former value refers to rms deviations and that the latter one refers to the number of superposed C atoms. The position of catalytic cysteine is indicated as a grey ball. (c) C trace of SSH2-C is superimposed with that of the VHR. The region cannot be aligned are colored green, whereas those of SSH2-C are missing are colored red. The point of view is the same as Figure 1(a). (d) The sliced view of active sites for SSH2-C and VHR. The molecular surface diagrams, which were produced using the program VOIDOO,[20] are drawn as a basket-weaved model. It shows the depth and width of the active site pocket for SSH-2C and VHR. The positions of catalytic cysteines are labeled in the figure.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 68, 408-412) copyright 2007.