Intersubunit Coupling Enables Fast CO2-Fixation by Reductive Carboxylases
Year: 2022
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide Enoyl-CoA carboxylases/reductases (ECRs) are some of the most efficient CO 2 -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 conformational coupling of catalytic domains is conferred by individual amino acids to achieve high CO 2 -fixation rates. Our results provide unprecedented insights into the dynamic organization and synchronized inter- and intrasubunit communications of this remarkably efficient CO 2 -fixing enzyme during catalysis.
Source: ACS Central Science
Authors: Hasan DeMirci, Yashas Rao, Gabriele M. Stoffel, Bastian Vögeli, Kristina Schell, Aharon Gomez, Alexander Batyuk, Cornelius Gati, Raymond G. Sierra, Mark S. Hunter, E. Han Dao, Halil I. Ciftci, Brandon Hayes, Fredric Poitevin, Po-Nan Li, Manat Kaur, Kensuke Tono, David Adrian Saez, Samuel Deutsch, Yasuo Yoshikuni, Helmut Grubmüller, Tobias J. Erb, Esteban Vöhringer-Martinez, Soichi Wakatsuki
Institutions: Koç University, SLAC National Accelerator Laboratory, University of Concepción, Max Planck Institute for Terrestrial Microbiology, Linac Coherent Light Source, Stanford University, SPring-8, Japan Synchrotron Radiation Research Institute, Lawrence Berkeley National Laboratory, Joint Genome Institute, Max Planck Institute for Multidisciplinary Sciences, Loewe Center for Synthetic Microbiology
Language: English
Subfield: Structural Biology
Domain: Life Sciences
SDG: Climate action
Open Access status: diamond
Funders: National Science Foundation, U.S. Department of Energy, Joint Genome Institute, Max-Planck-Gesellschaft, Türkiye Bilimsel ve Teknolojik Araştırma Kurumu, Ministry of Education, India, Office of Science, Stanford Precourt Institute for Energy, Comisión Nacional de Investigación Científica y Tecnológica, RIKEN, National Institute of General Medical Sciences, Office of Integrative Activities, Basic Energy Sciences, Biological and Environmental Research, Fondo Nacional de Desarrollo Científico y Tecnológico, H2020 European Research Council, SLAC National Accelerator Laboratory
Awards: G1014846411, G1229526393, G1286236842, G1286251239, G1414775356, G1445641779, G1451874870, G1816284028, G1863003419, G2371548206, G2539837713, G2618837358, G262532246, G2957134997, G303061748, G30714459, G3083819904, G365575497, G4099714421, G419881185, G4235786860, G42916606, G4501827968, G4581610328, G4599164271, G4654690619, G4908923434, G495301720, G498139845, G5570207115, G5849692847, Dinamik Yapısal Analiz Yöntemiyle Traf6 Proteininin Çinko Parmak Kısmına Bağlanan İnhibitörlerin Geliştirilmesi, G628751139, G6460157379, G650090426, G6550344761, G6652958823, G7083997402, G7205239661, G7283024673, G7313278570, G7322875612, G7762871514, G805243471, G834277795, G8382000481, G911061179, Biology with X-ray Lasers, G922851295, G969889393
OpenAlex ID: W4224862980