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. Author manuscript; available in PMC: 2022 Apr 27.
Published in final edited form as: Nat Struct Mol Biol. 2022 Jan 10;29(1):47–58. doi: 10.1038/s41594-021-00706-2

Extended Data Fig. 8 |. IMPDH1 retinal variant (546) is similar to canonical IMPDH1.

Extended Data Fig. 8 |

a-c, Active IMPDH1(546) filament bound to ATP, IMP, nAD+. a, Low-pass filtered cryo-EM reconstruction b, Interface-focused cryo-EM reconstruction. 8 monomers are colored by catalytic domain (green) and regulatory domain (pink). c, View of the top of an octamer from inside the filament. The surface area buried by the octamer interface is in aqua with the indicated total buried surface area. (Surface representation of the atomic model at the assembly interface, with buried residues in cyan). d-f, Inhibited IMPDH1(546) filament bound to GTP, ATP, IMP, nAD+. d, Low-pass filtered cryo-EM reconstruction e, Interface-focused cryo-EM reconstruction. 8 monomers are colored by catalytic domain (green) and regulatory domain (pink). f, View of the top of an octamer from inside the filament. The surface area buried by the octamer interface is in aqua with the indicated total buried surface area. (Surface representation of the atomic model at the assembly interface, with buried residues in cyan).