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Figure 1
Overall structures of the Vdh-F106V and Vdh-L348M mutants. (a, b) Ribbon diagrams of Vdh-F106V (a) and Vdh-L348M (b). The right-hand panels show the view from the proximal side, while the left panels show a view from the distal side of the haem cofactor. The two views are approximately 130° apart. The haem cofactor, the side chains of the mutated residue and Cys347 forming a coordinate bond to the haem iron are shown in stick representation. The α-­helices are labelled as per the established conventions for the P450 fold (αA–αK, αK′ and αL; Poulos et al., 1985BB36). (c) Main-chain superimposition of Vdh-F106V (green), Vdh-L348M (cyan) and Vdh-WT (yellow). The CD-loop moiety, where the main-chain conformational change is observed, is indicated by a red box.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 73| Part 5| May 2017| Pages 266-275
https://doi.org/10.1107/S2053230X17004782
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