9PFW
Crystal structure of selenomethionine-substituted N-oxygenase RohS from Pseudomonas syringae pv. tomato str. DC3000 (PstoRohS)
Summary for 9PFW
| Entry DOI | 10.2210/pdb9pfw/pdb |
| Related | 9PFX |
| Descriptor | Iron-containing redox enzyme family protein (2 entities in total) |
| Functional Keywords | azomycin, biosynthetic protein, n-oxygenase, heme-oxygenase-like enzyme |
| Biological source | Pseudomonas syringae pv. tomato str. DC3000 |
| Total number of polymer chains | 1 |
| Total formula weight | 35884.52 |
| Authors | |
| Primary citation | Wei, Z.W.,Salamon, P.,Higgins, M.A.,Ryan, K.S. Crystal structure of RohS, a heme-oxygenase-like N-oxygenase from azomycin biosynthesis. J.Biol.Chem., :111389-111389, 2026 Cited by PubMed Abstract: The nitro group is an important functional group found in the nitroimidazoles, antibiotic therapeutics for anaerobic pathogens. In the biosynthetic pathway to the nitroimidazole antibiotic azomycin, a nitro-forming enzyme RohS - a member of the heme-oxygenase-like dimetal/domain-containing oxidase/oxygenase (HDO) family - catalyzes a six-electron oxidation of 2-aminoimidazole to 2-nitroimidazole. Here we present the 2.20 Å resolution crystal structure of RohS and identify a potential active site pocket consisting of seven key residues important for metal coordination. By comparing the structures and sequences of two RohS homologs - one functionally active and one inactive - we convert the inactive RohS to its active form, thus revealing a key residue for metal coordination in RohS catalysis. Altogether, our work provides structural basis for further mechanistic investigation of this six-electron oxidation process and provides insight into the expanding repertoire of the HDO protein family and nitro-formation N-oxygenases. PubMed: 41866038DOI: 10.1016/j.jbc.2026.111389 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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