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TitleCooperativity in E. coli aspartate transcarbamoylase is tuned by allosteric breathing.
Journal, issue, pagesNat Commun, Year 2026
Publish dateMar 20, 2026
AuthorsRobert C Miller / Michael G Patterson / Neti Bhatt / Xiaokun Pei / Nozomi Ando /
PubMed AbstractAspartate transcarbamoylase (ATCase) from Escherichia coli catalyzes a key step in pyrimidine nucleotide biosynthesis and has long served as a model for allosteric regulation. Despite decades of ...Aspartate transcarbamoylase (ATCase) from Escherichia coli catalyzes a key step in pyrimidine nucleotide biosynthesis and has long served as a model for allosteric regulation. Despite decades of study, how nucleotide binding at distant regulatory sites controls cooperativity between active sites remained unresolved. Here we show that ATCase does not simply interconvert between two conformations, as traditionally depicted, but instead samples a continuum of conformations that tune enzyme cooperativity. Using complementary cryo-electron microscopy, small-angle X-ray scattering, and crystallography under conditions that ensure full assembly of the allosteric sites, we show that ATCase behaves like a flexible balloon whose global "breathing" motions directly regulate activity: compression enforces high cooperativity, inhibiting the enzyme, whereas expansion relieves this cooperativity and activates the enzyme. We further show that all four ribonucleoside triphosphates act in symmetric pairs to tune this motion, with the pyrimidines CTP and UTP compressing the enzyme to limit further pyrimidine production, and the purines ATP and GTP expanding it to balance pyrimidine and purine pools. Together, these findings uncover a dynamic breathing mechanism for long-range allosteric communication in ATCase.
External linksNat Commun / PubMed:41862478
MethodsEM (single particle)
Resolution3.85 Å
Structure data

47959

9een

EMDB-47959, PDB-9een:
Cryo-EM model of E. coli aspartate transcarbamoylase in the T-state complexed with CP, CTP, and Mg2+
Method: EM (single particle) / Resolution: 3.85 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CTP:
CYTIDINE-5'-TRIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-CP:
PHOSPHORIC ACID MONO(FORMAMIDE)ESTER

Source
  • escherichia coli (E. coli)
KeywordsCYTOSOLIC PROTEIN / Complex / Allostery / ATCase / R-State / CTP / UTP / CP / Succinate

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