Fig. 2: Architecture of MsmIMPDH.
From: Deciphering the allosteric regulation of mycobacterial inosine-5′-monophosphate dehydrogenase
a Side and top views of an MsmIMPDH octamer: the first tetramer is depicted in blue and gold, with its opposite tetramer in green and grey; the MsmIMPDH monomer is highlighted in saturated colours. b Structural details of the highlighted MsmIMPDH monomer. The catalytic domain is depicted in blue and the CBS domain in gold. The flexible loops of the Cys-loop (residues 320–326) are shown in orange, the finger (residues 391–404) in red, the flap (residues 405–450) in purple, and the IMP molecule in green. The two fingers and distal parts of the flaps form a binding interface between the two opposite protomers. c Four ATP molecules (in red) bound within Site 1 and 2 in a complex with four Mg2+ ions (in green) form an interface between two neighbouring CBS domains.
