1QNI
Crystal Structure of Nitrous Oxide Reductase from Pseudomonas nautica, at 2.4A Resolution
Summary for 1QNI
| Entry DOI | 10.2210/pdb1qni/pdb |
| Descriptor | NITROUS-OXIDE REDUCTASE, DINUCLEAR COPPER ION, (MU-4-SULFIDO)-TETRA-NUCLEAR COPPER ION, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, denitrification, mad, electron transfer |
| Biological source | PSEUDOMONAS NAUTICA |
| Total number of polymer chains | 6 |
| Total formula weight | 394554.76 |
| Authors | Brown, K.,Tegoni, M.,Cambillau, C. (deposition date: 1999-10-15, release date: 2000-10-13, Last modification date: 2024-05-08) |
| Primary citation | Brown, K.,Tegoni, M.,Prudencio, M.,Pereira, A.S.,Besson, S.,Moura, J.J.,Moura, I.,Cambillau, C. A novel type of catalytic copper cluster in nitrous oxide reductase. Nat.Struct.Biol., 7:191-195, 2000 Cited by PubMed Abstract: Nitrous oxide (N20) is a greenhouse gas, the third most significant contributor to global warming. As a key process for N20 elimination from the biosphere, N20 reductases catalyze the two-electron reduction of N20 to N2. These 2 x 65 kDa copper enzymes are thought to contain a CuA electron entry site, similar to that of cytochrome c oxidase, and a CuZ catalytic center. The copper anomalous signal was used to solve the crystal structure of N20 reductase from Pseudomonas nautica by multiwavelength anomalous dispersion, to a resolution of 2.4 A. The structure reveals that the CuZ center belongs to a new type of metal cluster, in which four copper ions are liganded by seven histidine residues. N20 binds to this center via a single copper ion. The remaining copper ions might act as an electron reservoir, assuring a fast electron transfer and avoiding the formation of dead-end products. PubMed: 10700275DOI: 10.1038/73288 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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