9pxf

Ammonia monooxygenase in native membranes from N. briensis

spinqualitylabelsall models 9pxf, resolution 2.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9pxf is a 9 chain structure with sequence from Nitrosospira briensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.58Å Ligands: 6PL, CU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1I5FI55_9PROT Publication Abstract from PubMed Ammonia monooxygenase (AMO), a copper-dependent membrane enzyme, catalyzes the first and rate-limiting step of nitrification: the oxidation of ammonia to hydroxylamine. Despite its central role in the global nitrogen cycle and its biotechnological relevance, structural characterization of AMO has lagged behind that of its homolog, particulate methane monooxygenase (pMMO), due to the slow growth rates of ammonia-oxidizing bacteria and the instability of AMO upon purification. Recent cryoEM studies of Nitrosomonas europaea AMO and Methylococcus capsulatus (Bath) pMMO in native membranes revealed new structural features, including two adjacent copper-binding sites in the transmembrane region, Cu(C) and Cu(D), believed to constitute the active site. Although multiple structures were determined under various conditions, simultaneous occupancy of Cu(C) and Cu(D) was never observed, leaving their potential functional interplay unresolved. Here we report the 2.6 A resolution cryoEM structure of AMO from Nitrosospira briensis C-128 in isolated native membranes. This structure reveals the first instance of simultaneous copper occupancy of the Cu(C) and Cu(D) sites, along with occupancy of the periplasmic Cu(B) site. Electron paramagnetic resonance (EPR) spectroscopic data indicate that the Cu(B) site is primarily occupied by Cu(ii), while Cu(C) and Cu(D) are primarily occupied by diamagnetic ions, presumably Cu(i). Notably, a lipid molecule is bound between the Cu(C) and Cu(D) sites, separating them by approximately 8.0 A. The results underscore the importance of studying these enzymes in their native environments across species to resolve conserved and divergent molecular features. Simultaneous occupancy of Cu(C) and Cu(D) in the ammonia monooxygenase active site.,Tucci FJ, Ho MB, Turner AAB, Stein LY, Hoffman BM, Rosenzweig AC Chem Sci. 2025 Dec 18. doi: 10.1039/d5sc08447d. PMID:41541579 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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