Extended Data Fig. 4: The comparison of SoBcmB complex structures. | Nature Catalysis

Extended Data Fig. 4: The comparison of SoBcmB complex structures.

From: Enzymatic catalysis favours eight-membered over five-membered ring closure in bicyclomycin biosynthesis

Extended Data Fig. 4: The comparison of SoBcmB complex structures.

a and b, The alignment of SoBcmB•FeII•αKG (orange) and SoBcmB•FeII•αKG•2 (slate), with r.m.s.d. value 0.2 Å. The inconsistent part is highlighted by the green box and the detail is shown in b. The key residue Y311 and D307 were missed in SoBcmB•FeII•αKG and highlighted by magenta dots. c, The alignment of SoBcmB•FeII•αKG•2 (slate) and SoBcmB·FeII·αKG·2a (yellow), with r.m.s.d. value 0.11 Å. d, The alignment of SoBcmB•FeII•αKG•2 (slate) and SoBcmB•FeII•αKG•2f (magenta) with r.m.s.d. value 0.11 Å. e, The alignment of SoBcmB•FeII•αKG•2 (slate) and SoBcmB•FeII•αKG•1 (cyangreen) with r.m.s.d. value 0.12 Å. f, The alignment of SoBcmB•FeII•αKG•1 (cyangreen) and SoBcmB•FeII•αKG•1d (pink), with r.m.s.d. value 0.14 Å. g, The alignment of SoBcmB•FeII•αKG•1 (cyangreen) and SoBcmB•FeII•αKG•1a (bluewhite), with r.m.s.d. value 0.18 Å. Substrates are shown as different coloured sticks. Water molecules are shown as different coloured spheres. The coordination bonds and the hydrogen bonds are labelled by yellow dash line.

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