Fig. 4: X-ray structure of the AmVHPO-R425S mutant in complex with 1,3,5-trimethoxybenzene (7, TMB). | Nature Communications

Fig. 4: X-ray structure of the AmVHPO-R425S mutant in complex with 1,3,5-trimethoxybenzene (7, TMB).

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

Fig. 4

a Ribbon diagram of dodecameric AmVHPO-R425S mutant with its surrogate TMB (7, one subunit is depicted in green, 7 and phosphate (PO43-) are shown as a ball-and-stick model with gold carbon atoms; PDB ID 8Q22). b Structural superposition of AmVHPO-R425S (green) and wild-type AmVHPO (tan, PDB ID 5LPC). Dots indicate a loop region that lacks defined electron density in the wild-type structure (residues 390–404, highlighted in cyan) but which adopts a defined motif in the mutant. c Surface cross-section of the AmVHPO-R425S variant in complex with 7. The cartoon represents one of 12 active sites in AmVHPO. The substrate binding pocket comprises two AmVHPO subunits shown in green and gray, respectively. Other subunits of the dodecamer are colored brown. Residue 425 (magenta) has a significant impact on the shape of the specificity pocket: TMB (7) is stabilized by a defined loop region from the adjacent subunit (residues 390–404, highlighted in cyan), which is fully resolved in R425S. AmVHPO = vanadium-dependent haloperoxidase from Acaryochloris marina.

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