Intersubunit Coupling Enables Fast CO₂-Fixation by Reductive Carboxylases.

ABSTRACT: 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 closed-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 conformationa

SUBMITTER: DeMirci H 

PROVIDER: S-EPMC9413435 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature