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TitleLarge-scale filament formation inhibits the activity of CTP synthetase.
Journal, issue, pagesElife, Vol. 3, Page e03638, Year 2014
Publish dateJul 16, 2014
AuthorsRachael M Barry / Anne-Florence Bitbol / Alexander Lorestani / Emeric J Charles / Chris H Habrian / Jesse M Hansen / Hsin-Jung Li / Enoch P Baldwin / Ned S Wingreen / Justin M Kollman / Zemer Gitai /
PubMed AbstractCTP Synthetase (CtpS) is a universally conserved and essential metabolic enzyme. While many enzymes form small oligomers, CtpS forms large-scale filamentous structures of unknown function in ...CTP Synthetase (CtpS) is a universally conserved and essential metabolic enzyme. While many enzymes form small oligomers, CtpS forms large-scale filamentous structures of unknown function in prokaryotes and eukaryotes. By simultaneously monitoring CtpS polymerization and enzymatic activity, we show that polymerization inhibits activity, and CtpS's product, CTP, induces assembly. To understand how assembly inhibits activity, we used electron microscopy to define the structure of CtpS polymers. This structure suggests that polymerization sterically hinders a conformational change necessary for CtpS activity. Structure-guided mutagenesis and mathematical modeling further indicate that coupling activity to polymerization promotes cooperative catalytic regulation. This previously uncharacterized regulatory mechanism is important for cellular function since a mutant that disrupts CtpS polymerization disrupts E. coli growth and metabolic regulation without reducing CTP levels. We propose that regulation by large-scale polymerization enables ultrasensitive control of enzymatic activity while storing an enzyme subpopulation in a conformationally restricted form that is readily activatable.
External linksElife / PubMed:25030911 / PubMed Central
MethodsEM (helical sym.)
Resolution8.4 Å
Structure data

EMDB-2700:
Cryo-EM structure of the CTP synthetase filament
Method: EM (helical sym.) / Resolution: 8.4 Å

Source
  • Escherichia coli (E. coli)

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