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TitleFilament formation drives catalysis by glutaminase enzymes important in cancer progression.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 1971, Year 2024
Publish dateMar 4, 2024
AuthorsShi Feng / Cody Aplin / Thuy-Tien T Nguyen / Shawn K Milano / Richard A Cerione /
PubMed AbstractThe glutaminase enzymes GAC and GLS2 catalyze the hydrolysis of glutamine to glutamate, satisfying the 'glutamine addiction' of cancer cells. They are the targets of anti-cancer drugs; however, their ...The glutaminase enzymes GAC and GLS2 catalyze the hydrolysis of glutamine to glutamate, satisfying the 'glutamine addiction' of cancer cells. They are the targets of anti-cancer drugs; however, their mechanisms of activation and catalytic activity have been unclear. Here we demonstrate that the ability of GAC and GLS2 to form filaments is directly coupled to their catalytic activity and present their cryo-EM structures which provide a view of the conformational states essential for catalysis. Filament formation guides an 'activation loop' to assume a specific conformation that works together with a 'lid' to close over the active site and position glutamine for nucleophilic attack by an essential serine. Our findings highlight how ankyrin repeats on GLS2 regulate enzymatic activity, while allosteric activators stabilize, and clinically relevant inhibitors block, filament formation that enables glutaminases to catalyze glutaminolysis and support cancer progression.
External linksNat Commun / PubMed:38438397 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution3.12 - 3.69 Å
Structure data

40918

8szj

EMDB-40918, PDB-8szj:
Human glutaminase C (Y466W) with L-Gln and Pi, filamentous form
Method: EM (helical sym.) / Resolution: 3.35 Å

40920

8szl

EMDB-40920, PDB-8szl:
Human liver-type glutaminase (Apo form)
Method: EM (single particle) / Resolution: 3.12 Å

40950

8t0z

EMDB-40950, PDB-8t0z:
Human liver-type glutaminase (K253A) with L-Gln, filamentous form
Method: EM (helical sym.) / Resolution: 3.3 Å

EMDB-43533: Human liver-type glutaminase, bound with inhibitor Compound 968
Method: EM (single particle) / Resolution: 3.69 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-GLN:
GLUTAMINE / Glutamine

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Cancer / Filament / Metabolism / Metabolic

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