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 | |
| 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., 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: 40644315DOI: 10.1021/jacs.5c04341 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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