Fig. 2: The structure of CEI-bound crystallographic homotetramer of NanoLuc luciferase.
From: Illuminating the mechanism and allosteric behavior of NanoLuc luciferase
a 2Fo-Fc electron density (contour level 1.2 σ) at the CEI-oxyluciferin binding site. b The overall structure of the NanoLuc homotetramer, composed of two tail-to-tail asymmetric homodimers (chain A in cyan, chain B in blue, chain C in violet and chain D in green). The CEI luciferin is shown as space-filling spheres (green). c Cutaway surface representation of CEI-bound NanoLuc tetramer. d Close-up views of CEI-binding pocket with residues creating the active site in stick representation. Key hydrogen bonds are shown as dashed yellow lines. e Superposition of FMA (yellow) and CEI (green) binding modes.
