Extended Data Fig. 4: Comparison between the Q-site in ForC (a) and HucS (b).
From: A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases
a. α-helices 223–236 and 240–257 of the ForC V-shape motif are represented in cartoon colored in dark blue with the side chain (T100 and E237). Electron transfer distance between the menaquinone and the His-coordinated [4Fe–4S] cluster is indicated. α-helices of ForE are colored in yellow and brown and numbered. b. α-helix 298–311 from the HucS subunit is represented in cartoon colored in dark blue and light blue for the two symmetry related molecules, with the side chain of Y301 and Y229 and the backbone carbonyl of K212. Electron transfer distance between the menaquinone and the distal [3Fe–4S] cluster is indicated. α-helices of HucM are colored in yellow and brown and numbered. a. and b. Clusters are represented in balls and sticks. Oxygen, sulfur and iron atoms are colored in red, yellow and brown respectively.
