Summary for 9LEG
| Entry DOI | 10.2210/pdb9leg/pdb |
| EMDB information | 63025 |
| Descriptor | Ammonia monooxygenase subunit A, COPPER (II) ION, [(2~{S})-2-hexadecanoyloxy-3-[methoxy(oxidanyl)phosphoryl]oxy-propyl] hexadecanoate, ... (13 entities in total) |
| Functional Keywords | amo complex, membrane protein |
| Biological source | Nitrosomonas halophila More |
| Total number of polymer chains | 15 |
| Total formula weight | 393058.70 |
| Authors | |
| Primary citation | Yang, X.,Li, Z.,Mao, T.Q.,Ma, C.,Chen, G.H.,Dong, H.P.,Sui, S.F. Structural insights into the catalytic mechanism of ammonia monooxygenase. Nat Commun, 17:508-508, 2025 Cited by PubMed Abstract: Ammonia monooxygenase (AMO) oxidizes ammonia to hydroxylamine. Limited knowledge of the structural information of AMO hinders our understanding of the molecular mechanism underlying ammonia oxidation, impacting the mitigation of greenhouse gas emissions and enhancing agricultural productivity using ammonium as a nitrogen source. Herein, we report the cryo-electron microscopy structure of the AMO complex from an isolated strain of ammonia-oxidizing bacteria (AOB). AMO is a cylinder-shaped homotrimeric assembly composed of five subunits. A single-transmembrane protein and a soluble protein are potentially crucial in signal transduction during ammonia oxidation and mediating interactions with the outer membrane protein assembly machinery. Three modeled coppers, along with an adjacent water-mediated hydrogen-bond network, may facilitate an efficient proton transfer pathway from the periplasmic Cu to the active site Cu within the inner membrane, where Cu and Cu will act in concert to catalyze substrate reaction. The distinctive surface charge characteristics of AMO provide valuable insights into the structural features that govern ammonium assimilation and material transport during ammonia oxidation. These findings shed light on the molecular complexities of AMO and provides a structural foundation for elucidating the catalytic mechanism of ammonia oxidation. PubMed: 41387732DOI: 10.1038/s41467-025-67194-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.36 Å) |
Structure validation
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