1FGJ
X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE
Summary for 1FGJ
| Entry DOI | 10.2210/pdb1fgj/pdb |
| Descriptor | HYDROXYLAMINE OXIDOREDUCTASE, PROTOPORPHYRIN IX CONTAINING FE, HEME C (3 entities in total) |
| Functional Keywords | oxidoreductase, nitrification |
| Biological source | Nitrosomonas europaea |
| Cellular location | Periplasm: Q50925 |
| Total number of polymer chains | 2 |
| Total formula weight | 133340.75 |
| Authors | Tanaka, N.,Igarashi, N.,Moriyama, H. (deposition date: 1997-03-03, release date: 1998-03-04, Last modification date: 2024-11-13) |
| Primary citation | Igarashi, N.,Moriyama, H.,Fujiwara, T.,Fukumori, Y.,Tanaka, N. The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Nat.Struct.Biol., 4:276-284, 1997 Cited by PubMed Abstract: The 2.8 A crystal structure of hydroxylamine oxidoreductase of a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea, is described. Twenty-four haems lie in the centre bottom of the trimeric molecule, localized in four clusters within each monomer. The haem clusters within the trimer are aligned to form a ring that has inlet and outlet sites. The inlet is occupied by a novel haem, P460, and there are two possible outlet sites per monomer formed by paired haems lying within a cavity or cleft on the protein surface. The structure suggests pathways by which electron transfer may occur through the precisely arranged haems and provides a framework for the interpretation of previous and future biochemical and genetic observations. PubMed: 9095195DOI: 10.1038/nsb0497-276 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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