6fwf

Low resolution structure of Neisseria meningitidis qNOR

spinqualitylabelsall models 6fwf, resolution 4.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fwf is a 1 chain structure. This structure supersedes the now removed PDB entry 6elh. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, FE, HEM Related: 6elh Activity: Nitric-oxide reductase (cytochrome c), with EC number 1.7.2.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bacterial nitric oxide reductases (NORs) catalyse the reduction of NO to N2O and H2O. NORs are found either in denitrification chains, or in pathogens where their primary role is detoxification of NO produced by the immune defense of the host. Although NORs belong to the heme-copper oxidase superfamily, comprising proton-pumping O2-reducing enzymes, the best studied NORs, cNORs (cytochrome c-dependent), are non-electrogenic. Here, we focus on another type of NOR, qNOR (quinol-dependent). Recombinant qNOR from Neisseria meningitidis, a human pathogen, purified from Escherichia coli, showed high catalytic activity and spectroscopic properties largely similar to cNORs. However, in contrast to cNOR, liposome-reconstituted qNOR showed respiratory control ratios above two, indicating that NO reduction by qNOR was electrogenic. Further, we determined a 4.5 A crystal structure of the N. meningitidis qNOR, allowing exploration of a potential proton transfer pathway from the cytoplasm by mutagenesis. Most mutations had little effect on the activity, however the E-498 variants were largely inactive, while the corresponding substitution in cNOR was previously shown not to induce significant effects. We thus suggest that, contrary to cNOR, the N. meningitidis qNOR uses cytoplasmic protons for NO reduction. Our results allow possible routes for protons to be discussed. Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.,Gonska N, Young D, Yuki R, Okamoto T, Hisano T, Antonyuk S, Hasnain SS, Muramoto K, Shiro Y, Tosha T, Adelroth P Sci Rep. 2018 Feb 26;8(1):3637. doi: 10.1038/s41598-018-21804-0. PMID:29483528 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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