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Published January 1, 2022 | Version v1
Journal article Open

Intersubunit Coupling Enables Fast CO2-Fixation by Reductive Carboxylases

Creators

  • 1. Max Planck Inst Terr Microbiol, Dept Biochem & Synthet Metab, D-35043 Marburg, Germany
  • 2. Univ Concepcion, Fac Ciencias Quim, Dept Fis Quim, Concepcion 4030000, Chile
  • 3. SLAC Natl Accelerator Lab, Linac Coherent Light Source, Menlo Pk, CA 94025 USA
  • 4. SLAC Natl Accelerator Lab, PULSE Inst, Menlo Pk, CA 94025 USA
  • 5. Stanford Univ, Struct Biol Dept, Stanford, CA 94305 USA
  • 6. US DOE, Joint Genome Inst, Lawrence Berkeley Natl Lab, Walnut Creek, CA 94720 USA

Description

Enoyl-CoA carboxylases/reductases (ECRs) are some of the most efficient CO2-fixing enzymes described to date. However, the molecular mechanisms underlying the extraordinary catalytic activity of ECRs on the level of the protein assembly remain elusive. Here we used a combination of ambient-temperature X-ray free electron laser (XFEL) and cryogenic synchrotron experiments to study the structural organization of the ECR from Kitasatospora setae. The K. setae ECR is a homotetramer that differentiates into a pair of dimers of open- and dosed-form subunits in the catalytically active state. Using molecular dynamics simulations and structure-based mutagenesis, we show that catalysis is synchronized in the K. setae ECR across the pair of dimers. This conformational coupling of catalytic domains is conferred by individual amino acids to achieve high CO2-fixation rates. Our results provide unprecedented insights into the dynamic organization and synchronized inter- and intrasubunit communications of this remarkably efficient CO2-fixing enzyme during catalysis.

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