Fig. 2: hsALAS2 C-terminal extension is mobile and interferes directly with active site. | Nature Communications

Fig. 2: hsALAS2 C-terminal extension is mobile and interferes directly with active site.

From: Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

Fig. 2

a Interactions of helix α15 from the Ct-extension (dark green) with the catalytic core of monomer A shown in light green and the opposing monomer B shown in yellow. b Similar view as panel A, related by 30° rotation along the horizontal axis. The succinyl-CoA (sCoA) ligand, modeled into hsALAS2 from rcALAS (PDB 2BWO), is shown in black lines to highlight steric clashes with helix α15. c hsALAS2 monomer with catalytic domain in surface representation (light green) and Ct-extension in cartoon representation (dark green). The scALAS Ct-extension is also superimposed in cartoon representation (gray). d rcALAS (PDB 2BWN), scALAS (PDB 5TXR) and hsALAS2 (this study) homodimers. Catalytic domains are shown in surface representation (monomer A light green, monomer B yellow). Ct-extensions are shown in cartoon representation for scALAS and rcALAS (dark green for monomer A, orange for monomer B).

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