3O0R
Crystal structure of nitric oxide reductase from Pseudomonas aeruginosa in complex with antibody fragment
Summary for 3O0R
| Entry DOI | 10.2210/pdb3o0r/pdb |
| Descriptor | antibody fab fragment light chain, antibody fab fragment heavy chain, Nitric oxide reductase subunit B, ... (10 entities in total) |
| Functional Keywords | oxidoreductase, electron transport, heme, iron, membrane, cytoplasmic membrane, immune system-oxidoreductase complex, immune system/oxidoreductase |
| Biological source | Mus musculus More |
| Cellular location | Cell membrane; Multi-pass membrane protein (Potential): Q59647 Cell membrane; Single-pass membrane protein: Q59646 |
| Total number of polymer chains | 4 |
| Total formula weight | 118379.16 |
| Authors | Hino, T.,Matsumoto, Y.,Nagano, S.,Sugimoto, H.,Fukumori, Y.,Murata, T.,Iwata, S.,Shiro, Y. (deposition date: 2010-07-20, release date: 2010-12-29, Last modification date: 2024-10-30) |
| Primary citation | Hino, T.,Matsumoto, Y.,Nagano, S.,Sugimoto, H.,Fukumori, Y.,Murata, T.,Iwata, S.,Shiro, Y. Structural basis of biological N2O generation by bacterial nitric oxide reductase Science, 330:1666-1670, 2010 Cited by PubMed Abstract: Nitric oxide reductase (NOR) is an iron-containing enzyme that catalyzes the reduction of nitric oxide (NO) to generate a major greenhouse gas, nitrous oxide (N(2)O). Here, we report the crystal structure of NOR from Pseudomonas aeruginosa at 2.7 angstrom resolution. The structure reveals details of the catalytic binuclear center. The non-heme iron (Fe(B)) is coordinated by three His and one Glu ligands, but a His-Tyr covalent linkage common in cytochrome oxidases (COX) is absent. This structural characteristic is crucial for NOR reaction. Although the overall structure of NOR is closely related to COX, neither the D- nor K-proton pathway, which connect the COX active center to the intracellular space, was observed. Protons required for the NOR reaction are probably provided from the extracellular side. PubMed: 21109633DOI: 10.1126/science.1195591 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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