Fig. 1: Domain organization and structure of hsALAS2. | Nature Communications

Fig. 1: Domain organization and structure of hsALAS2.

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

Fig. 1

a Domain architecture of hsALAS1, hsALAS2, scALAS, and rcALAS, highlighting the catalytic core (gray box) flanked by N-terminal (black, pink boxes) and C-terminal extension (green in higher eukaryotes, orange in lower eukaryotes). b hsALAS2 homodimer (this study) composed of monomer A (catalytic domain in gray, Ct-extension in dark green) and the opposite monomer B (catalytic domain in yellow, Ct-extension in orange. PLP is shown in purple sticks. c Structure superimposition of protomer from hsALAS2 (this study), scALAS (PDB 5TXR) and rcALAS (PDB 2BWN). d Domain organization and secondary structure assignment for hsALAS2. Subdomain 1 is shown in pink, subdomain 2 in gray, subdomain 3 in cyan, and the Ct-extension in dark green. e PLP binding site of hsALAS2. PLP-interacting residues from monomer A are shown in gray and from opposing monomer B in yellow. PLP is shown in mauve (carbon color).

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