4p1c
From Proteopedia
CRYSTAL STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE HYDROXYLASE-FERREDOXIN C7S, C84A, C85A VARIANT ELECTRON-TRANSFER COMPLEX
Structural highlights
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 PubMedProductive 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. References
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