Figure 5From: Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor bindingSchematic view on possible dimer structures of styrene monooxygenase components. StyA has the same fold as PHBH and the domains were accordingly colored (Montersino et al. 2011, 2013; Schreuder et al. 1988). FAD binding domain in green, substrate binding domain in red, and dimer interface in blue. The three-dimensional structure of StyA from Pseudomonas sp. S12 (PDB ID: 3IHM, Ukaegbu et al. 2010) is shown in a, where the active site clefts of monomers point to the center and no PHBH-like dimer was determined. A modelled StyA-dimer is presented in b. Here the dimer interfaces interact in a flavoprotein hydroxylase mode (Montersino et al. 2013; Schreuder et al. 1988) and a ‘back to back’ situation is shown in which active sites point into the medium. The experimentally solved three-dimensional StyB-structure (PDB ID: 4F07, Morrison et al. 2013) is shown as dimer in (c). Together the structures of a and c were used to generate a model of StyA2B (d) in which two dimer interfaces occur (van den Heuvel et al. 2004). For clarity, only one StyA2B monomer is shown.Back to article page