Human IMPDH2 treated with ATP, IMP, and 20 mM GTP. Fully compressed filament end reconstruction.

Cryo-EM structures demonstrate human IMPDH2 filament assembly tunes allosteric regulation.

Inosine-5'-monophosphate dehydrogenase 2

SEFELMADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTE
AGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLV
GIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPL
ASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLID
AGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTE
APGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKS
LTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

metabolism, filament, allostery, adenine, guanine, BIOSYNTHETIC PROTEIN

MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAI
AMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISS
RDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDA
KKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDA
LRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEY
FFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVR
AMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF

binding site for Di-peptide ATP A 605 and ARG A 161
binding site for Di-peptide ATP C 605 and ARG C 161
binding site for Di-peptide GTP E 602 and LYS E 208
binding site for Di-peptide GTP F 602 and LYS F 208
binding site for Di-peptide GTP G 602 and LYS G 208
binding site for Di-peptide GTP H 602 and LYS H 208