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Crystal Structure of 4-Hydroxybutyryl-CoA Synthetase (ADP-forming): A Key Enzyme in the Thaumarchaeal Hydroxypropionate/Hydroxybutyrate cycle

By Hasan Demirci1, J Johnson, Bradley Tolar, Bilge Tosun, Yasuo Yoshikuni, Christopher Francis, Soichi Wakatsuki

1. Biosciences Division at SLAC National Accelerator Laboratory

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Category

BioXFEL Publications

Published on

Type

posted-content

Author

Hasan DeMirci and J Johnson and Bradley Tolar and Bilge Tosun and Yasuo Yoshikuni and Christopher Francis and Soichi Wakatsuki

Citation

DeMirci, H., Johnson, J., Tolar, B., Tosun, B., Yoshikuni, Y., Francis, C., & Wakatsuki, S. (2023). Crystal Structure of 4-Hydroxybutyryl-CoA Synthetase (ADP-forming): A Key Enzyme in the Thaumarchaeal Hydroxypropionate/Hydroxybutyrate cycle. https://doi.org/10.21203/rs.3.rs-3173078/v1

Abstract

Abstract The 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle from ammonia-oxidizing Thaumarchaeota is currently considered the most energy-efficient aerobic carbon fixation pathway. The Nitrosopumilus maritimus 4-hydroxybutyryl-CoA synthetase (ADP-forming) (Nmar_0206) from this cycle represents one of a number of proteins that exhibit increased efficiency over its crenarchaeal counterparts. Nmar_0206 catalyzes the conversion of 4-hydroxybutyrate (4HB) and Coenzyme-A (CoA) to 4-hydroxybutyryl-CoA through the dephosphorylation of ATP to ADP, as opposed to AMP as seen in Crenarchaeota. This enzyme reduces energy requirements on the cell, thus reflecting thaumarchaeal success in adapting to low-nutrient environments.

DOI

http://dx.doi.org/10.21203/rs.3.rs-3173078/v1

Funding

NSF-STC Biology with X-ray Lasers (NSF-1231306)