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TitleA Nucleotide-Dependent Conformational Switch Controls the Polymerization of Human IMP Dehydrogenases to Modulate their Catalytic Activity.
Journal, issue, pagesJ Mol Biol, Vol. 431, Issue 5, Page 956-969, Year 2019
Publish dateMar 1, 2019
AuthorsDavid Fernández-Justel / Rafael Núñez / Jaime Martín-Benito / David Jimeno / Adrián González-López / Eva María Soriano / José Luis Revuelta / Rubén M Buey /
PubMed AbstractInosine 5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate-limiting step in the de novo GTP biosynthetic pathway and plays essential roles in cell proliferation. As a clinical target, IMPDH ...Inosine 5'-monophosphate dehydrogenase (IMPDH) catalyzes the rate-limiting step in the de novo GTP biosynthetic pathway and plays essential roles in cell proliferation. As a clinical target, IMPDH has been studied for decades, but it has only been within the last years that we are starting to understand the complexity of the mechanisms of its physiological regulation. Here, we report structural and functional insights into how adenine and guanine nucleotides control a conformational switch that modulates the assembly of the two human IMPDH enzymes into cytoophidia and allosterically regulates their catalytic activity. In vitro reconstituted micron-length cytoophidia-like structures show catalytic activity comparable to unassembled IMPDH but, in turn, are more resistant to GTP/GDP allosteric inhibition. Therefore, IMPDH cytoophidia formation facilitates the accumulation of high levels of guanine nucleotides when the cell requires it. Finally, we demonstrate that most of the IMPDH retinopathy-associated mutations abrogate GTP/GDP-induced allosteric inhibition and alter cytoophidia dynamics.
External linksJ Mol Biol / PubMed:30664871
MethodsEM (helical sym.) / X-ray diffraction
Resolution2.567 - 24.0 Å
Structure data

EMDB-4402:
Electron microscopy map of human IMPDH isoform 1 bound to GDP in 150 g/L Ficoll-70
Method: EM (helical sym.) / Resolution: 18.0 Å

EMDB-4403:
Electron microscopy map of human IMPDH isoform 1 bound to ATP in 150 g/L Ficoll-70
Method: EM (helical sym.) / Resolution: 24.0 Å

PDB-6i0m:
Structure of human IMP dehydrogenase, isoform 2, bound to GDP
Method: X-RAY DIFFRACTION / Resolution: 2.567 Å

PDB-6i0o:
Structure of human IMP dehydrogenase, isoform 2, bound to GTP
Method: X-RAY DIFFRACTION / Resolution: 2.623 Å

Chemicals

ChemComp-5GP:
GUANOSINE-5'-MONOPHOSPHATE

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

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

Source
  • homo sapiens (human)
KeywordsBIOSYNTHETIC PROTEIN / oxidoreductase / de novo guanine nucleotide biosynthesis

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