2BMR
The Crystal Structure of Nitrobenzene Dioxygenase in complex with 3- nitrotoluene
Summary for 2BMR
| Entry DOI | 10.2210/pdb2bmr/pdb |
| Related | 2BMO 2BMQ |
| Descriptor | OXYGENASE-ALPHA NBDO, OXYGENASE-BETA NBDO, FE2/S2 (INORGANIC) CLUSTER, ... (9 entities in total) |
| Functional Keywords | nitrobenzene dioxygenase, nitroarene, rieske non-heme dioxygenase, substrate specificity iron-sulfur, metal-binding, nad, oxidoreductase |
| Biological source | COMAMONAS SP. More |
| Total number of polymer chains | 2 |
| Total formula weight | 74009.84 |
| Authors | Friemann, R.,Ivkovic-Jensen, M.M.,Lessner, D.J.,Yu, C.,Gibson, D.T.,Parales, R.E.,Eklund, H.,Ramaswamy, S. (deposition date: 2005-03-15, release date: 2005-05-04, Last modification date: 2023-12-13) |
| Primary citation | Friemann, R.,Ivkovic-Jensen, M.M.,Lessner, D.J.,Yu, C.L.,Gibson, D.T.,Parales, R.E.,Eklund, H.,Ramaswamy, S. Structural insight into the dioxygenation of nitroarene compounds: the crystal structure of nitrobenzene dioxygenase. J. Mol. Biol., 348:1139-1151, 2005 Cited by PubMed Abstract: Nitroaromatic compounds are used extensively in many industrial processes and have been released into the environment where they are considered environmental pollutants. Nitroaromatic compounds, in general, are resistant to oxidative attack due to the electron-withdrawing nature of the nitro groups and the stability of the benzene ring. However, the bacterium Comamonas sp. strain JS765 can grow with nitrobenzene as a sole source of carbon, nitrogen and energy. Biodegradation is initiated by the nitrobenzene dioxygenase (NBDO) system. We have determined the structure of NBDO, which has a hetero-hexameric structure similar to that of several other Rieske non-heme iron dioxygenases. The catalytic subunit contains a Rieske iron-sulfur center and an active-site mononuclear iron atom. The structures of complexes with substrates nitrobenzene and 3-nitrotoluene reveal the structural basis for its activity with nitroarenes. The substrate pocket contains an asparagine residue that forms a hydrogen bond to the nitro-group of the substrate, and orients the substrate in relation to the active-site mononuclear iron atom, positioning the molecule for oxidation at the nitro-substituted carbon. PubMed: 15854650DOI: 10.1016/j.jmb.2005.03.052 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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