Fig. 3: Substrate ISP-ED binding to the substrate-binding cavity is detected only in the ADP state. | Nature Communications

Fig. 3: Substrate ISP-ED binding to the substrate-binding cavity is detected only in the ADP state.

From: Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate

Fig. 3

A Three final classes from the mBcs1L/ISP-ED data set are shown in cut-away view (top) exposing the interior content of the substrate-binding cavity and the view from the bottom (bottom). From left to right: experimental map of mBcs1L (green) bound with ISP-ED (yellow); surface rendition of the mBcs1L model (green) and modeled ISP-ED (yellow); the experimental map of ADP-bound mBcs1L without ISP-ED (Blue); the experimental map of mBcs1L in ATP state-2 (magenta); and the map from apo mBcs1L (purple) as a control. All reconstructions were performed in C1 symmetry. B Surface representation of mBcs1L bound with ISP-ED shown in different orientations. A model of ADP-state mBcs1L was fit into the map using ChimeraX, followed by fitting a model of bovine ISP-ED (1rie.pdb) into the extra density in the matrix cavity using the Emplace_local tool via ChimeraX. The sharpened local map generated by Emplace_local is shown as semi-transparent surface.

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