8ztz

Structure of ATP-dependent diazotase CmaA6

spinqualitylabelsall models 8ztz, resolution 2.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ztz is a 5 chain structure with sequence from Kutzneria albida DSM 43870. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.93Å Ligands: AMP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W5W4E6_9PSEU Publication Abstract from PubMed Although several diazotases have been recently reported, the details of the reaction mechanism are not yet understood. In this study, we investigated the mechanism of CmaA6, an ATP-dependent diazotase, which catalyzes the diazotization of 3-aminocoumaric acid using nitrous acid. X-ray crystallography and cryogenic electron microscopy-single particle analysis revealed CmaA6 structures in the substrate-free and AMP-binding states. Kinetic analysis suggested that CmaA6 catalyzes diazotization via a sequential reaction mechanism in which three substrates (nitrous acid, ATP, and 3-aminocoumaric acid) are simultaneously bound in the reaction pocket. The nitrous acid and 3-aminocoumaric acid binding sites were predicted based on the AMP-binding state and confirmed by site-directed mutagenesis. In addition, computational analysis revealed a tunnel for 3-aminocoumaric acid to enter the reaction pocket, which was advantageous for the sequential reaction mechanism. This study provides important insights into the catalytic mechanism of diazotization in natural product biosynthesis. Structural Basis for the Catalytic Mechanism of ATP-Dependent Diazotase CmaA6.,Kawai S, Karasawa M, Moriwaki Y, Terada T, Katsuyama Y, Ohnishi Y Angew Chem Int Ed Engl. 2025 Apr 24:e202505851. doi: 10.1002/anie.202505851. PMID:40275441 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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