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

DeMirci, H., Rao, Y., Stoffel, G. M., Vögeli, B., Schell, K., Gomez, A., et al. (2022). Inter-subunit coupling enables fast CO2-fixation by reductive carboxylases. ACS Central Science, In Press. doi:10.1021/acscentsci.2c00057.

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DeMirci, H., Author
Rao, Y., Author
Stoffel, G. M., Author
Vögeli, B., Author
Schell, K., Author
Gomez , A., Author
Batyuk, A., Author
Gati, C., Author
Sierra, R. G., Author
Hunter, M. S., Author
Dao, E. H., Author
Ciftci, H. I., Author
Hayes, B., Author
Poitevin, F., Author
Li, P.-N., Author
Kaur, M., Author
Tono, K., Author
Saez, D. A., Author
Deutsch, S., Author
Yoshikuni, Y., Author
Grubmüller, H.1, Author              Erb, T. J., AuthorVöhringer-Martinez, E.1, Author              Wakatsuki, S., Author more..
Affiliations:
1Department of Theoretical and Computational Biophysics, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society, ou_3350132              

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 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 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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Language(s): eng - English
 Dates: 2022-01-192022-03-312022-04-25
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/acscentsci.2c00057
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Title: ACS Central Science
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: In Press Start / End Page: - Identifier: -