Figure 5

Scheme describing the differences in oligomerization. (A) The Cα's from 2 conserved leucine residues (i.e. Leu 102 and Leu139) are shown for Pv Trx-Px1. Two dimers are highlighted: the first comprised of blue and green monomers and second comprised of yellow and orange monomers. (B) The Cα's from 2 conserved leucine residues are shown (i.e. Leu96 and Leu133 in Py Trx-Px1). Two dimers are highlighted: the first comprised of green and purple monomers and second comprised of yellow and blue monomers. (C) The same spheres are shown from (A) from a different angle and scale with a grey line connecting the Lys's of the same monomer for clarity. The distances and angles calculated (by Pymol) in the next panel are defined. Note that these were made for the sole purpose of comparing the orientation of the monomers within the structure at the B-type interface and at the A-type interface. (D) Summary table showing the average distances and angles calculated for each of the measurements indicated in the previous panel. The standard deviations are not shown for clarity, but are less than 0.5% in each case.