9ODT

The structure of a Bacterial Cyanide Dihydratase from Bacillus safensis PER-URP-08

Summary for 9ODT

• Entry DOI: 10.2210/pdb9odt/pdb
• EMDB information: 70376
• Descriptor: Cyanide dihydratase (1 entity in total)
• Functional Keywords: cynd, nitrilase, biorremediation, oligomer, hydrolase
• Biological source: Bacillus safensis
• Total number of polymer chains: 18
• Total formula weight: 675472.01

Authors

Justo Arevalo, S.,Valle-Riestra F, V.,Balan, A.,Chuck, C.S. (deposition date: 2025-04-27, release date: 2026-02-25)

Primary citation

Justo Arevalo, S.,Valle-Riestra Felice, V.,Barahona Acuna, M.,Ordinola Flores, K.,Quinones Aguilar, M.,Balan, A.,Farah, C.S.
The single-particle cryo-EM structures of a bacterial cyanide dihydratase and a fungal cyanide hydratase.
Structure, 2026

PubMed Abstract: Cyanide is widely used in industries due to its affinity for metals, a property that also underlies its toxicity. Industries, therefore, must reduce cyanide concentration before the final disposal of wastewater. Physical, chemical, and biological methods have been developed for this; however, knowledge about the structure of enzymes involved in cyanide degradation remains limited. Structural characterization of these proteins could facilitate the development of enzymes with enhanced bioremediation potential. Here, we present the single-particle cryo-electron microscopy structures of a cyanide dihydratase from Bacillus safensis and a cyanide hydratase from Gloeocercospora sorghi at 2.2 Å and 2.0 Å resolution, respectively. We provide a comprehensive description and comparative analysis alongside all previously determined nitrilase structures. Importantly, our full-length structures reveal new features in the C-terminal as well as specific intermolecular interactions between protomer interfaces and within the helix lumen. Finally, our findings offer insights into the reaction mechanisms of these two enzymes.

PubMed: 41709456
DOI: 10.1016/j.str.2026.01.009

Experimental method

ELECTRON MICROSCOPY (2.04 Å)