9C5W

Crystal structure of cyclodehydratase RohQ in complex with imidazole

Summary for 9C5W

Entry DOI	10.2210/pdb9c5w/pdb
Descriptor	Cyclodehydratase RohQ, IMIDAZOLE (3 entities in total)
Functional Keywords	azomycin biosynthetic protein, duf6190, cyclodehydratase, de novo emerged enzyme, biosynthetic protein
Biological source	Pseudomonas brassicacearum
Total number of polymer chains	5
Total formula weight	99141.12
Authors	Wei, Z.-W.,Ryan, K.S. (deposition date: 2024-06-06, release date: 2025-07-23, Last modification date: 2025-08-06)
Primary citation	Wei, Z.W.,Daniel-Ivad, P.,Zhang, L.,Ryan, K.S. Structure and Mechanism of the Azomycin Biosynthetic Enzyme RohQ That Catalyzes a Spontaneous Cyclodehydration. J.Am.Chem.Soc., 147:25117-25122, 2025 Cited by PubMed Abstract: RohQ from the azomycin biosynthetic pathway catalyzes a spontaneous cyclodehydration to form 2-aminoimidazole. Here we report the structure and mechanism of RohQ and use a serendipitously bound imidazole to pinpoint active site residues. We propose that catalysis occurs at the dimeric interface using two key aspartic acid residues for proton transfer steps to accelerate 3 × 10-fold intramolecular cyclization of a guanidino group and aldehyde, releasing water. Our work expands our understanding of emerged enzymes and provides the first structural and mechanistic view of a yet-unexplored protein family. PubMed: 40644315 DOI: 10.1021/jacs.5c04341 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation