Figure 3

3D architecture of DXR-II showing relevant and functional divergence residues. A, view of the DXR-II dimer. Chain A is represented as cartoon backbone highlighting secondary structures and chain B as its molecular surface equivalent. B, Close-up view of the active site and of residues participating in substrate/fosmidomycin binding, including position 229, also predicted as related to functional divergence. C, Close-up view of the cavity at the dimer interface highlighting conserved residues involved in interactions between the two subunits of the DXR-II dimer, including position 320, also predicted as related to functional divergence. The N-terminal, central and C-terminal domains are shown in grey, blue and cyan, respectively. Residues predicted as involved in functional divergence of DXR-II are shown in red. Residues identified as involved in dimerization, fosmidomycin/substrate binding and the active site are shown in yellow, violet and green, respectively. The competitive inhibitor fosmidomycin is colored in orange. Molecular graphics were produced with VMD 1.9.1 [29] on the basis of the crystal structure of B. abortus DXR-II (pdb: 3upy) [26].