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TitleIMPDH1 retinal variants control filament architecture to tune allosteric regulation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 1, Page 47-58, Year 2022
Publish dateJan 10, 2022
AuthorsAnika L Burrell / Chuankai Nie / Meerit Said / Jacqueline C Simonet / David Fernández-Justel / Matthew C Johnson / Joel Quispe / Rubén M Buey / Jeffrey R Peterson / Justin M Kollman /
PubMed AbstractInosine-5'-monophosphate dehydrogenase (IMPDH), a key regulatory enzyme in purine nucleotide biosynthesis, dynamically assembles filaments in response to changes in metabolic demand. Humans have two ...Inosine-5'-monophosphate dehydrogenase (IMPDH), a key regulatory enzyme in purine nucleotide biosynthesis, dynamically assembles filaments in response to changes in metabolic demand. Humans have two isoforms: IMPDH2 filaments reduce sensitivity to feedback inhibition, while IMPDH1 assembly remains uncharacterized. IMPDH1 plays a unique role in retinal metabolism, and point mutants cause blindness. Here, in a series of cryogenic-electron microscopy structures we show that human IMPDH1 assembles polymorphic filaments with different assembly interfaces in extended and compressed states. Retina-specific splice variants introduce structural elements that reduce sensitivity to GTP inhibition, including stabilization of the extended filament form. Finally, we show that IMPDH1 disease mutations fall into two classes: one disrupts GTP regulation and the other has no effect on GTP regulation or filament assembly. These findings provide a foundation for understanding the role of IMPDH1 in retinal function and disease and demonstrate the diverse mechanisms by which metabolic enzyme filaments are allosterically regulated.
External linksNat Struct Mol Biol / PubMed:35013599 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 3.9 Å
Structure data

24437

7rer

EMDB-24437, PDB-7rer:
HUMAN IMPDH1 TREATED WITH ATP, IMP, AND NAD+
Method: EM (single particle) / Resolution: 2.6 Å

24438

7res

EMDB-24438: HUMAN IMPDH1 TREATED WITH ATP, IMP, AND NAD+; OCTAMER-CENTERED
PDB-7res: HUMAN IMPDH1 TREATED WITH ATP, IMP, AND NAD+, OCTAMER-CENTERED
Method: EM (single particle) / Resolution: 3.05 Å

24439

7rfe

EMDB-24439, PDB-7rfe:
HUMAN IMPDH1 TREATED WITH GTP, IMP, AND NAD+; INTERFACE-CENTERED
Method: EM (single particle) / Resolution: 2.6 Å

24440

7rff

EMDB-24440, PDB-7rff:
HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH ATP; INTERFACE-CENTERED
Method: EM (single particle) / Resolution: 2.7 Å

24441

7rfg

EMDB-24441, PDB-7rfg:
HUMAN IMPDH1 TREATED WITH GTP, IMP, AND NAD+ OCTAMER-CENTERED
Method: EM (single particle) / Resolution: 2.6 Å

24442

7rfh

EMDB-24442, PDB-7rfh:
HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH ATP, OCTAMER-CENTERED
Method: EM (single particle) / Resolution: 3.7 Å

24443

7rfi

EMDB-24443, PDB-7rfi:
HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH GTP, ATP, IMP, NAD+, INTERFACE-CENTERED
Method: EM (single particle) / Resolution: 2.6 Å

24448

7rgd

EMDB-24448, PDB-7rgd:
HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH GTP, ATP, IMP, NAD+, OCTAMER-CENTERED
Method: EM (single particle) / Resolution: 3.0 Å

24450

7rgi

EMDB-24450, PDB-7rgi:
HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH GTP, ATP, IMP, NAD+; INTERFACE-CENTERED
Method: EM (single particle) / Resolution: 3.6 Å

24451

7rgl

EMDB-24451, PDB-7rgl:
HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH ATP, IMP, NAD+, INTERFACE-CENTERED
Method: EM (single particle) / Resolution: 2.4 Å

24452

7rgm

EMDB-24452, PDB-7rgm:
HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH ATP, IMP, NAD+, OCTAMER-CENTERED
Method: EM (single particle) / Resolution: 2.8 Å

24454

7rgq

EMDB-24454, PDB-7rgq:
HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH GTP, ATP, IMP, NAD+; INTERFACE-CENTERED
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-IMP:
INOSINIC ACID

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / METABOLISM / FILAMENT / ALLOSTERY / ADENINE

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