Structural highlights
4p1c is a 8 chain structure with sequence from Atcc 25411. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , |
| Gene: | tmoA (ATCC 25411), tmoE (ATCC 25411), tmoB (ATCC 25411), tmoC (ATCC 25411) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[TMOC_PSEME] Probable electron transfer from NADPH, via FAD and the 2Fe-2S center, to the oxygenase activity site of the enzyme. [TMOA_PSEME] Hydroxylase subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.[1] [2] [TMOB_PSEME] Subunit T4moB of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.[3] [4] [TMOE_PSEME] Subunit of the multicomponent enzyme toluene-4-monooxygenase that hydroxylates toluene to form p-cresol.
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ 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
- ↑ 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:http://dx.doi.org/10.1038/ncomms6009
