5OC0
Structure of E. coli superoxide oxidase
Summary for 5OC0
| Entry DOI | 10.2210/pdb5oc0/pdb |
| Descriptor | Cytochrome b561, PROTOPORPHYRIN IX CONTAINING FE, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | membrane protein, superoxide, electron transport, heme, respiratory chain, ros, quinone, ubiquinone, oxidoreductase |
| Biological source | Escherichia coli K12 |
| Total number of polymer chains | 1 |
| Total formula weight | 24278.98 |
| Authors | Lundgren, C.A.K.,Sjostrand, D.,Biner, O.,Bennett, M.,von Ballmoos, C.,Hogbom, M. (deposition date: 2017-06-29, release date: 2018-06-20, Last modification date: 2024-11-06) |
| Primary citation | Lundgren, C.A.K.,Sjostrand, D.,Biner, O.,Bennett, M.,Rudling, A.,Johansson, A.L.,Brzezinski, P.,Carlsson, J.,von Ballmoos, C.,Hogbom, M. Scavenging of superoxide by a membrane-bound superoxide oxidase. Nat. Chem. Biol., 14:788-793, 2018 Cited by PubMed Abstract: Superoxide is a reactive oxygen species produced during aerobic metabolism in mitochondria and prokaryotes. It causes damage to lipids, proteins and DNA and is implicated in cancer, cardiovascular disease, neurodegenerative disorders and aging. As protection, cells express soluble superoxide dismutases, disproportionating superoxide to oxygen and hydrogen peroxide. Here, we describe a membrane-bound enzyme that directly oxidizes superoxide and funnels the sequestered electrons to ubiquinone in a diffusion-limited reaction. Experiments in proteoliposomes and inverted membranes show that the protein is capable of efficiently quenching superoxide generated at the membrane in vitro. The 2.0 Å crystal structure shows an integral membrane di-heme cytochrome b poised for electron transfer from the P-side and proton uptake from the N-side. This suggests that the reaction is electrogenic and contributes to the membrane potential while also conserving energy by reducing the quinone pool. Based on this enzymatic activity, we propose that the enzyme family be denoted superoxide oxidase (SOO). PubMed: 29915379DOI: 10.1038/s41589-018-0072-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.97 Å) |
Structure validation
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