| Structural highlights
4p1b is a 8 chain structure with sequence from Pseudomonas mendocina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.05Å |
| Ligands: | ACT, FE, FES, NA, PEG |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
TMOA_ECTME Component of the toluene-4-monooxygenase multicomponent enzyme system which catalyzes the O2- and NADH-dependent hydroxylation of toluene to form p-cresol (PubMed:15240250, PubMed:1885512, PubMed:19290655, PubMed:19705873, PubMed:2019563). Also able to convert benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by successive hydroxylations (PubMed:15240250).[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Productive biomolecular recognition requires exquisite control of affinity and specificity. Accordingly, nature has devised many strategies to achieve proper binding interactions. Bacterial multicomponent monooxygenases provide a fascinating example, where a diiron hydroxylase must reversibly interact with both ferredoxin and catalytic effector in order to achieve electron transfer and O2 activation during catalysis. Because these two accessory proteins have distinct structures, and because the hydroxylase-effector complex covers the entire surface closest to the hydroxylase diiron centre, how ferredoxin binds to the hydroxylase has been unclear. Here we present high-resolution structures of toluene 4-monooxygenase hydroxylase complexed with its electron transfer ferredoxin and compare them with the hydroxylase-effector structure. These structures reveal that ferredoxin or effector protein binding produce different arrangements of conserved residues and customized interfaces on the hydroxylase in order to achieve different aspects of catalysis.
Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system.,Acheson JF, Bailey LJ, Elsen NL, Fox BG Nat Commun. 2014 Sep 24;5:5009. doi: 10.1038/ncomms6009. PMID:25248368[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tao Y, Fishman A, Bentley WE, Wood TK. Oxidation of benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-monooxygenase of Ralstonia pickettii PKO1. Applied and environmental microbiology. 2004 Jul 1. doi: 10.1128/AEM.70.7.3814-3820.2004. PMID: 15240250.
- ↑ Yen KM, Karl MR, Blatt LM, Simon MJ, Winter RB, Fausset PR, Lu HS, Harcourt AA, Chen KK. Cloning and characterization of a Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase. Journal of bacteriology. 1991 Sep 1. doi: 10.1128/jb.173.17.5315-5327.1991. PMID: 1885512.
- ↑ Elsen NL, Bailey LJ, Hauser AD, Fox BG. Role for threonine 201 in the catalytic cycle of the soluble diiron hydroxylase toluene 4-monooxygenase. Biochemistry. 2009 May 12;48(18):3838-46. PMID:19290655 doi:10.1021/bi900144a
- ↑ Bailey LJ, Fox BG. Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase. Biochemistry. 2009 Sep 29;48(38):8932-9. PMID:19705873 doi:10.1021/bi901150a
- ↑ Whited GM, Gibson DT. Toluene-4-monooxygenase, a three-component enzyme system that catalyzes the oxidation of toluene to p-cresol in Pseudomonas mendocina KR1. Journal of bacteriology. 1991 May 1. doi: 10.1128/jb.173.9.3010-3016.1991. PMID: 2019563.
- ↑ Acheson JF, Bailey LJ, Elsen NL, Fox BG. Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system. Nat Commun. 2014 Sep 24;5:5009. doi: 10.1038/ncomms6009. PMID:25248368 doi:https://dx.doi.org/10.1038/ncomms6009
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