Fig. 6: Exposure of the active site cofactor to the surface in different VHPOs. | Nature Communications

Fig. 6: Exposure of the active site cofactor to the surface in different VHPOs.

From: Unraveling the molecular basis of substrate specificity and halogen activation in vanadium-dependent haloperoxidases

Fig. 6

The bromoperoxidases wild-type AmVHPO (PDB: 5LPC), CoVHPO (PDB: 1QHB), and CpVHPO (PDB: 1UP8) and the chlorinating enzymes AnVHPO (PDB: 1QI9), CiVHPO (PDB: 1IDQ), NapH1 (PDB: 3W36) are compared. Enzymes are depicted as dimeric units (gray and light green), except CiVHPO (PDB: 1IDQ), which mainly acts as a monomer. In the case of the dodecamers wild-type AmVHPO (PDB: 5LPC), CoVHPO (PDB: 1QHB), and CpVHPO (PDB: 1UP8), a combination of two subunits was chosen that resembles the densest packing around the prosthetic vanadate and phosphate group, respectively (blue spheres). VHPO = vanadium-dependent haloperoxidase; AmVHPO = vanadium-dependent haloperoxidase from Acarychloris marina; CoVHPO = vanadium-dependent haloperoxidase from Corallina officinalis; CpVHPO = vanadium-dependent haloperoxidase from Corallina pilulifera; AnVHPO = vanadium-dependent haloperoxidase from Ascophyllum nodosum; CiVHPO = vanadium-dependent haloperoxidase from Curvularia inaequalis; NapH1 = vanadium-dependent napyradiomycin haloperoxidase from Streptomyces sp. CNQ-525.

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