8bgw | pdb_00008bgw

CryoEM structure of quinol-dependent Nitric Oxide Reductase (qNOR) from Alcaligenes xylosoxidans at 2.2 A resolution

spinqualitylabelsall models 8bgw, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8bgw is a 2 chain structure with sequence from Achromobacter xylosoxidans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.2Å Ligands: 10M, CA, FE, HEM, LOP, UQ1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0D6H8R3_ALCXX Publication Abstract from PubMed Quinol-dependent nitric oxide reductases (qNORs) are considered members of the respiratory heme-copper oxidase superfamily, are unique to bacteria, and are commonly found in pathogenic bacteria where they play a role in combating the host immune response. qNORs are also essential enzymes in the denitrification pathway, catalysing the reduction of nitric oxide to nitrous oxide. Here, we determine a 2.2 A cryoEM structure of qNOR from Alcaligenes xylosoxidans, an opportunistic pathogen and a denitrifying bacterium of importance in the nitrogen cycle. This high-resolution structure provides insight into electron, substrate, and proton pathways, and provides evidence that the quinol binding site not only contains the conserved His and Asp residues but also possesses a critical Arg (Arg720) observed in cytochrome bo(3), a respiratory quinol oxidase. A 2.2 A cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases.,Flynn AJ, Antonyuk SV, Eady RR, Muench SP, Hasnain SS Nat Commun. 2023 Jun 9;14(1):3416. doi: 10.1038/s41467-023-39140-x. PMID:37296134 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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