Structural highlights
3en1 is a 2 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , |
| Related: | 3dqy, 3ef6, 3eqq |
| Gene: | bnzA, TodA, todC1 ("Bacillus fluorescens putidus" Flugge 1886), bnzB, TodB, todC2 ("Bacillus fluorescens putidus" Flugge 1886) |
| Activity: | Toluene dioxygenase, with EC number 1.14.12.11 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
Function
[BNZA_PSEPU] Catalyzes both the oxidation of benzene and toluene. [BNZB_PSEPU] Catalyzes both the oxidation of benzene and toluene. The beta subunit may be responsible for the substrate specificity of the enzyme.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacterial Rieske non-heme iron oxygenases catalyze the initial hydroxylation of aromatic hydrocarbon substrates. The structures of all three components of one such system, the toluene 2,3-dioxygenase system, have now been determined. This system consists of a reductase, a ferredoxin and a terminal dioxygenase. The dioxygenase, which was cocrystallized with toluene, is a heterohexamer containing a catalytic and a structural subunit. The catalytic subunit contains a Rieske [2Fe-2S] cluster and mononuclear iron at the active site. This iron is not strongly bound and is easily removed during enzyme purification. The structures of the enzyme with and without mononuclear iron demonstrate that part of the structure is flexible in the absence of iron. The orientation of the toluene substrate in the active site is consistent with the regiospecificity of oxygen incorporation seen in the product formed. The ferredoxin is Rieske type and contains a [2Fe-2S] cluster close to the protein surface. The reductase belongs to the glutathione reductase family of flavoenzymes and consists of three domains: an FAD-binding domain, an NADH-binding domain and a C-terminal domain. A model for electron transfer from NADH via FAD in the reductase and the ferredoxin to the terminal active-site mononuclear iron of the dioxygenase is proposed.
Structures of the multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system.,Friemann R, Lee K, Brown EN, Gibson DT, Eklund H, Ramaswamy S Acta Crystallogr D Biol Crystallogr. 2009 Jan;65(Pt 1):24-33. Epub 2008, Dec 18. PMID:19153463[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Friemann R, Lee K, Brown EN, Gibson DT, Eklund H, Ramaswamy S. Structures of the multicomponent Rieske non-heme iron toluene 2,3-dioxygenase enzyme system. Acta Crystallogr D Biol Crystallogr. 2009 Jan;65(Pt 1):24-33. Epub 2008, Dec 18. PMID:19153463 doi:10.1107/S0907444908036524
