3AYF
Crystal structure of nitric oxide reductase
Summary for 3AYF
| Entry DOI | 10.2210/pdb3ayf/pdb |
| Related | 3AYG |
| Descriptor | Nitric oxide reductase, PROTOPORPHYRIN IX CONTAINING FE, ZINC ION, ... (8 entities in total) |
| Functional Keywords | oxidoreductase |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 95150.89 |
| Authors | Matsumoto, Y.,Tosha, T.,Pisliakov, A.V.,Hino, T.,Sugimoti, H.,Nagano, S.,Sugita, Y.,Shiro, Y. (deposition date: 2011-05-06, release date: 2012-01-25, Last modification date: 2024-03-13) |
| Primary citation | Matsumoto, Y.,Tosha, T.,Pisliakov, A.V.,Hino, T.,Sugimoto, H.,Nagano, S.,Sugita, Y.,Shiro, Y. Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus Nat.Struct.Mol.Biol., 19:238-245, 2012 Cited by PubMed Abstract: The structure of quinol-dependent nitric oxide reductase (qNOR) from G. stearothermophilus, which catalyzes the reduction of NO to produce the major ozone-depleting gas N(2)O, has been characterized at 2.5 Å resolution. The overall fold of qNOR is similar to that of cytochrome c-dependent NOR (cNOR), and some structural features that are characteristic of cNOR, such as the calcium binding site and hydrophilic cytochrome c domain, are observed in qNOR, even though it harbors no heme c. In contrast to cNOR, structure-based mutagenesis and molecular dynamics simulation studies of qNOR suggest that a water channel from the cytoplasm can serve as a proton transfer pathway for the catalytic reaction. Further structural comparison of qNOR with cNOR and aerobic and microaerobic respiratory oxidases elucidates their evolutionary relationship and possible functional conversions. PubMed: 22266822DOI: 10.1038/nsmb.2213 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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