1o7p
From Proteopedia
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| , resolution 1.95Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | Naphthalene 1,2-dioxygenase, with EC number 1.14.12.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NAPHTHALENE 1,2-DIOXYGENASE, PRODUCT COMPLEX
Overview
Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.
About this Structure
1O7P is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron., Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S, Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937
Page seeded by OCA on Sun Mar 30 22:41:03 2008
Categories: Naphthalene 1,2-dioxygenase | Protein complex | Pseudomonas putida | Eklund, H. | Gibson, D T. | Karlsson, A. | Parales, J V. | Parales, R E. | Ramaswamy, S. | Aromatic hydrocarbon catabolism oxidoreductase | Enzyme-substrate complex | Iron-sulfur | Non-heme iron dioxygenase | Oxidoreductase
