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Figure 5
(a) Ribbon diagram of the CYP105D18 structure. Rainbow coloring from blue to red indicates the N- to C-terminal positions of residues in the model. The right panel is rotated by 90° relative to the left panel, such that the side of the substrate-binding funnel in the right panel orients toward the reader in the left panel. The nomenclature of the secondary helices and β-sheets was chosen from previous studies. (b) Multiple sequence alignment with other homologous CYPs. CYP105D18 from S. laurentii, CYP105D7 and CYP105D6/PteD from Streptomyces sp., CYP105D6 from S. avermitilis, CYP105N1 from S. coelicolor, CYP105A1 from S. griseolus, CYP105AB3 from Nonomuraea recticatena, GfsF from S. gramino­faciens, CYP105AS1 from Amycolatopsis orientalis, and CYP105P1 from S. avermitilis. Secondary structural elements are shown above the aligned sequences and colored according to the scheme in Fig. 5[link](a). Regions for the active site are marked with orange sticks, and conserved residues at the B/C loop and turn of αF–αG are marked by red circles.

Volume 8| Part 4| July 2021| Pages 684-694
ISSN: 2052-2525