Fig. 2 (IMAGE)

Osaka University

Fig. 2

Caption

Model of QhpC/QhpD/QhpG ternary complex. In this complex, QhpC is triply crosslinked at the active-site pocket of QhpD, along with [4Fe4S] clusters. Subsequently, a specific Trp residue of the crosslinked QhpC becomes dihydroxylated at the active site of QhpG close to the FAD. The complex formation thus enables efficient and sequential posttranslational modifications.

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Osaka University

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