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. 2022 Aug 29;17(9):2643–2654. doi: 10.1021/acschembio.2c00575

Figure 1.

Figure 1

Structure of OaPAC and the flavin binding pocket. (A) OaPAC is a homodimer composed of a BLUF domain (cyan color) linked to an AC domain (sand color) responsible for converting ATP into cAMP and PPi in a light-dependent manner (PDB: 5x4t).18 (B) Hydrogen-bonding network that surrounds the isoalloxazine ring of the FAD. The structure of OaPAC (cyan) has been superimposed on the structure of AppA (yellow; PDB: 1YRX) where the tryptophan (W104) is in the Trpin conformation.12 Residue numbers are for AppA, while those in parentheses are for OaPAC.