4P1C

CRYSTAL STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE HYDROXYLASE-FERREDOXIN C7S, C84A, C85A VARIANT ELECTRON-TRANSFER COMPLEX

Summary for 4P1C

• Entry DOI: 10.2210/pdb4p1c/pdb
• Descriptor: Toluene-4-monooxygenase system protein A, Toluene-4-monooxygenase system protein E, Toluene-4-monooxygenase system protein B, ... (8 entities in total)
• Functional Keywords: electron-transfer complex, oxidoreductase, diiron enzyme complex, iron-sulfur, reduction, hydroxylase ferredoxin, oxygenase
• Biological source: Pseudomonas mendocina; More
• Total number of polymer chains: 8
• Total formula weight: 229759.77

Authors

Acheson, J.F.,Fox, B.G. (deposition date: 2014-02-25, release date: 2014-10-01, Last modification date: 2023-09-27)

Primary citation

Acheson, J.F.,Bailey, L.J.,Elsen, N.L.,Fox, B.G.
Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system.
Nat Commun, 5:5009-5009, 2014

PubMed Abstract: 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.

PubMed: 25248368
DOI: 10.1038/ncomms6009

Experimental method

X-RAY DIFFRACTION (2.4 Å)