Inter-subunit coupling enables fast CO₂-fixation by reductive carboxylases

Journal Article · Fri Apr 12 00:00:00 EDT 2019

OSTI ID:1863955

DeMirci, Hasan ^[1]; Rao, Yashas ^[2]; Stoffel, Gabriele M. ^[3]; Vogeli, Bastian ^[3]; Schell, Kristina ^[3]; Gomez, Aharon ^[4]; Batyuk, Alexander ^[5]; Gati, Cornelius ^[6]; Sierra, Raymond G. ^[5]; Hunter, Mark S. ^[5]; Dao, E. Han ^[7]; Ciftci, Halil I. ^[8]; Hayes, Brandon ^[5]; Poitevin, Fredric ^[5]; Li, Po-Nan ^[9]; Kaur, Manat ^[6]; Tono, Kensuke ^[10]; Saez, David Adrian ^[11]; Deutsch, Samuel ^[12]; Yoshikuni, Yasuo ^[12] ; Grubmuller, Helmut ^[13]; Erb, Tobias J. ^[3]; Vohringer-Martinez, Esteban ^[4]; Wakatsuki, Soichi ^[14]

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1. SLAC National Accelerator Lab., Menlo Park, CA (United States). Biosciences Div.; SLAC National Accelerator Lab., Menlo Park, CA (United States). Photon Ultrafast Laser Science and Engineering Inst. (PULSE); Koc Univ., Istanbul (Turkey). Dept. of Molecular Biology and Genetics
2. SLAC National Accelerator Lab., Menlo Park, CA (United States). Biosciences Div.; Universidad de Concepcion (Chili). Dept. de Fisico Quimica, Facultad de Ciencias Quimicas
3. Max Planck Inst. for Terrestrial Microbiology, Marburg (Germany). Dept. of Biochemistry and Synthetic Metabolism
4. Universidad de Concepcion (Chili). Dept. de Fisico Quimica, Facultad de Ciencias Quimicas
5. SLAC National Accelerator Lab., Menlo Park, CA (United States). Linac Coherent Light Source (LCLS)
6. Stanford Univ., CA (United States). Structural Biology Dept.
7. SLAC National Accelerator Lab., Menlo Park, CA (United States). Biosciences Div.; SLAC National Accelerator Lab., Menlo Park, CA (United States). Photon Ultrafast Laser Science and Engineering Inst. (PULSE)
8. SLAC National Accelerator Lab., Menlo Park, CA (United States). Photon Ultrafast Laser Science and Engineering Inst. (PULSE)
9. SLAC National Accelerator Lab., Menlo Park, CA (United States). Biosciences Div.; Stanford Univ., CA (United States). Electrical Engineering Dept.
10. RIKEN SPring-8 Center, Sayo, Hyogo (Japan); Japan Synchrotron Radiation Research Institute, Sayo, Hyogo (Japan)
11. Universidad de Concepcion (Chili). Dept. de Fisico Quimica, Facultad de Ciencias Quimicas; Universidad de Concepcion (Chili). Departamento de Farmacia, Facultad de Farmacia
12. USDOE Joint Genome Institute (JGI), Walnut Creek, CA (United States)
13. Max Planck Inst. for Biophysical Chemistry, Gottingen (Germany). Dept. of Theoretical and Computational Biophysics
14. SLAC National Accelerator Lab., Menlo Park, CA (United States). Biosciences Div.; Stanford Univ., CA (United States). Structural Biology Dept.

Enoyl-CoA carboxylases/reductases (ECRs) belong to the most efficient CO 2 -fixing enzymes described to date. However, the molecular mechanisms underlying ECR’s extraordinary catalytic activity 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. K. setae ECR is a homo-tetramer that differentiates into a dimer 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 K. setae ECR across the pair of two 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 intra-subunit communications of this remarkably efficient CO 2 -fixing enzyme during catalysis.

• Research Organization: SLAC National Accelerator Lab., Menlo Park, CA (United States)
• Sponsoring Organization: USDOE Office of Science (SC), Basic Energy Sciences (BES)
• DOE Contract Number: AC02-76SF00515; AC02-05CH11231; NSF-1231306; 118C270; 120Z520; ERC 637675; 21190252; CONICYT PCI MPG190003; 3190579
• OSTI ID: 1863955
• Country of Publication: United States
• Language: English