1FWX
CRYSTAL STRUCTURE OF NITROUS OXIDE REDUCTASE FROM P. DENITRIFICANS
Summary for 1FWX
| Entry DOI | 10.2210/pdb1fwx/pdb |
| Related | 1qni |
| Descriptor | NITROUS OXIDE REDUCTASE, CHLORIDE ION, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | beta-propeller domain, cupredoxin domain, cuz site, cua site, oxidoreductase |
| Biological source | Paracoccus denitrificans |
| Cellular location | Periplasm: Q51705 |
| Total number of polymer chains | 4 |
| Total formula weight | 267826.03 |
| Authors | Brown, K.,Djinovic-Carugo, K.,Haltia, T.,Cabrito, I.,Saraste, M.,Moura, J.J.,Moura, I.,Tegoni, M.,Cambillau, C. (deposition date: 2000-09-25, release date: 2001-09-25, Last modification date: 2023-08-09) |
| Primary citation | Brown, K.,Djinovic-Carugo, K.,Haltia, T.,Cabrito, I.,Saraste, M.,Moura, J.J.,Moura, I.,Tegoni, M.,Cambillau, C. Revisiting the Catalytic CuZ Cluster of Nitrous Oxide (N2O) Reductase. Evidence of a Bridging Inorganic Sulfur J.Biol.Chem., 275:41133-41136, 2000 Cited by PubMed Abstract: Nitrous-oxide reductases (N2OR) catalyze the two-electron reduction of N(2)O to N(2). The crystal structure of N2ORs from Pseudomonas nautica (Pn) and Paracoccus denitrificans (Pd) were solved at resolutions of 2.4 and 1.6 A, respectively. The Pn N2OR structure revealed that the catalytic CuZ center belongs to a new type of metal cluster in which four copper ions are liganded by seven histidine residues. A bridging oxygen moiety and two other hydroxide ligands were proposed to complete the ligation scheme (Brown, K., Tegoni, M., Prudencio, M., Pereira, A. S., Besson, S., Moura, J. J. G., Moura, I., and Cambillau, C. (2000) Nat. Struct. Biol. 7, 191-195). However, in the CuZ cluster, inorganic sulfur chemical determination and the high resolution structure of Pd N2OR identified a bridging inorganic sulfur instead of an oxygen. This result reconciles the novel CuZ cluster with the hitherto puzzling spectroscopic data. PubMed: 11024061DOI: 10.1074/jbc.M008617200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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