5tdu

Toluene 4-monooxygenase (T4moHD) bound to product after turnover in crystal

spinqualitylabelsall models 5tdu, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tdu is a 4 chain structure with sequence from Atcc 25411. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, PCR Related: 5tds, 5tdt, 5tdv Gene: tmoA (ATCC 25411), tmoE (ATCC 25411), tmoB (ATCC 25411), tmoD (ATCC 25411) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TMOD_PSEME] Effector protein subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. Required for optimal efficiency and specificity of the holoenzyme. [TMOA_PSEME] Hydroxylase subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. [TMOB_PSEME] Subunit T4moB of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. [TMOE_PSEME] Subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol. Publication Abstract from PubMed Electrophilic aromatic substitution is one of the most important and recognizable classes of organic chemical transformation. Enzymes create the strong electrophiles that are needed for these highly energetic reactions by using O2, electrons, and metals or other cofactors. Although the nature of the oxidants that carry out electrophilic aromatic substitution has been deduced from many approaches, it has been difficult to determine their structures. Here we show the structure of a diiron hydroxylase intermediate formed during a reaction with toluene. Density functional theory geometry optimizations of an active site model reveal that the intermediate is an arylperoxo Fe2+/Fe3+ species with delocalized aryl radical character. The structure suggests that a carboxylate ligand of the diiron centre may trigger homolytic cleavage of the O-O bond by transferring a proton from a metal-bound water. Our work provides the spatial and electronic constraints needed to propose a comprehensive mechanism for diiron enzyme arene hydroxylation that accounts for many prior experimental results. In-crystal reaction cycle of a toluene-bound diiron hydroxylase.,Acheson JF, Bailey LJ, Brunold TC, Fox BG Nature. 2017 Mar 27. doi: 10.1038/nature21681. PMID:28346937 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase 3D structures

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