FIGURE 2.
A, a stereo view representation of the superposition of Tpa1N (light brown) on Tpa1C (blue) is shown. B, a surface representation of residue conservation mapped at the surface of the Tpa1C domain is shown. Coloring is from blue (highly conserved) to gray (low conservation). C, Tpa1C interacting surface with Tpa1N is shown. D, a ribbon representation of the Tpa1 homodimer observed in the crystal is shown. One monomer is shown in blue, and the other one is in green. Tpa1N and Tpa1C are in light and dark colors, respectively. E, surface representation of residue conservation mapped at the surface of Tpa1 homodimer is shown (same color code as Fig. 2A). F, size-exclusion chromatography as followed by a triple detector array of Tpa1 is shown. For clarity only, the UV absorption (280 nm) for the eluted sample (left y axis) and molecular mass calculated from light scattering (right y axis, logarithmic scale) are shown. mAU, milliabsorbance units. G, shown is a surface representation of Tpa1 active site (same color code as Fig. 2A) with the HIFα CODD (yellow) and (Ser-Pro)5 (pink) peptides shown in ribbon. The hydroxylated proline is shown in sticks. The iron atom is shown as a black sphere. H, the representation is the same as panel G. Tpa1N and Tpa1C are colored gray and beige, respectively. The βB-βC β-hairpin is shown in green.