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. 2022 Apr 27;31(5):e4314. doi: 10.1002/pro.4314

FIGURE 3.

FIGURE 3

Structure of PaIMPDH bound to ATP and GDP. Detailed views of ATP (a) and GDP (b) bound in the Bateman domain to the first and second nucleotide canonical sites, respectively. IMPDH protein is represented in semitransparent blue cartoons with the side chain of key interacting residues shown in sticks. The 2mFo–DFc electron density map, contoured at the 1.6σ level, is shown as a grey mesh. Key protein–nucleotide atomic interactions are represented as orange dashed lines and the coordinated Magnesium atom is shown as an orange sphere. (c) Upper panel: structural superposition of the catalytic domains (white ribbons) of a monomer of PaIMPDH showing the different conformations adopted by the Bateman domain upon ATP (orange ribbons; PDB ID 4DQW) 10 or ATP/GDP (blue ribbons) binding. Lower panel: the conformational switch described in the upper panel, translated to the octameric structures. PaIMPDH octamers are represented as protein surfaces with the same color code as in the upper panel. IMPDH, IMP dehydrogenase; PaIMPDH, Pseudomonas aeruginosa IMPDH