Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus
Category
Published on
Type
journal-article
Author
Jerome Johnson and Bradley B. Tolar and Bilge Tosun and Yasuo Yoshikuni and Christopher A. Francis and Soichi Wakatsuki and Hasan DeMirci
Citation
Johnson, J., Tolar, B. B., Tosun, B., Yoshikuni, Y., Francis, C. A., Wakatsuki, S., & DeMirci, H. (2024). Crystal structure of the 4-hydroxybutyryl-CoA synthetase (ADP-forming) from nitrosopumilus maritimus. Communications Biology, 7(1). https://doi.org/10.1038/s42003-024-06432-x
Abstract
AbstractThe 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) represents one of several enzymes from this cycle that exhibit increased efficiency over crenarchaeal counterparts. This enzyme reduces energy requirements on the cell, reflecting thaumarchaeal success in adapting to low-nutrient environments. Here we show the structure of Nmar_0206 from Nitrosopumilus maritimus SCM1, which reveals a highly conserved interdomain linker loop between the CoA-binding and ATP-grasp domains. Phylogenetic analysis suggests the widespread prevalence of this loop and highlights both its underrepresentation within the PDB and structural importance within the (ATP-forming) acyl-CoA synthetase (ACD) superfamily. This linker is shown to have a possible influence on conserved interface interactions between domains, thereby influencing homodimer stability. These results provide a structural basis for the energy efficiency of this key enzyme in the modified 3HP/4HB cycle of Thaumarchaeota.
DOI
Funding
NSF-STC Biology with X-ray Lasers (NSF-1231306)
