9oqu | pdb_00009oqu

N-hydroxylamine dehydratase (NohD) T98A/K167A mutant crystal structure with heme and N-hydroxylated ornithine (5h soak)

spinqualitylabelsall models 9oqu, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9oqu is a 2 chain structure with sequence from Actinomadura. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.73Å Ligands: HEM, ONH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Enzymes that form nitrogen-nitrogen bonds are employed in natural product biosynthesis and the nitrogen cycle. Piperazate synthase forms the cyclic hydrazine l-piperazic acid from l-N(5)-OH-ornithine, using heme as a cofactor. In this work, we discover sequence-related enzyme NohD that instead reacts with l-N(5)-OH-ornithine to release ammonia, and we solve its structure to 1.4 A resolution. We then employ structure-guided site-directed mutagenesis to endow variants of NohD with piperazate synthase activity. Crystal structures of the NohD variants reveal how the heme propionate changes conformation, positioning it upward toward the amino nitrogen, where it is likely to activate the amine for N-N bond-formation. This study highlights a key structural requirement for N-N bond-formation and sets the stage for the development of new N-N-bond-forming catalysts. Conversion of a Heme-Dependent Dehydratase to a Piperazate Synthase Reveals the Role of the Heme Propionate Group in N-N Bond-Formation.,Higgins MA, Mirotadze N, Shi X, Hoffarth ER, Du YL, Ryan KS J Am Chem Soc. 2025 Oct 29;147(43):39160-39168. doi: 10.1021/jacs.5c08886. Epub , 2025 Oct 16. PMID:41101755 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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