Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system

• DOI: 10.1038/ncomms6009
• Publication Date: 2014-09-24T11:00:05Z
• Authors: Justin F. Acheson; Lucas J. Bailey; Nathaniel L. Elsen; Brian G. Fox
• Keywords: Models, Molecular; 0303 health sciences; Binding Sites; Protein Conformation; Ferric Compounds; Article; Catalysis; Mixed Function Oxygenases; 03 medical and health sciences; Multiprotein Complexes; Escherichia coli; Oxygenases; Ferredoxins; Electrophoresis, Polyacrylamide Gel; Cloning, Molecular; Crystallization

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 diiron hydroxylase must reversibly interact with both ferredoxin catalytic effector in order electron transfer O 2 activation during catalysis. Because these two accessory proteins have distinct structures, because the hydroxylase-effector complex covers entire surface closest centre, how binds been unclear. Here we present high-resolution structures toluene 4-monooxygenase complexed its compare them structure. These reveal that or protein produce different arrangements conserved residues customized interfaces on aspects