Fig. 1: Structural and Functional characterization of outward open human ABCD1.
From: Structures of the human peroxisomal fatty acid transporter ABCD1 in a lipid environment
a ATPase activity of ABCD1 reconstituted in liposomes or nanodiscs as a function of ATP concentration, n = 3 and error bars represent standard deviation b ATPase activity of DDM/CHS detergent purified ABCD1 in the presence of CoA esters of the indicated varying acyl chain composition, normalized to ABCD1’s basal rate at left, n = 6 (100 µM) or 3 (1 mM) and error bars represent S.E.M. Statistical significance by unpaired, two-tailed t-test p-values of <0.05, 0.01, 0.001, 0.0001 are indicated by *, **, ***, ****, respectively. c−f Map and structure of human ABCD1 outward open (OO) homodimer viewed from the membrane plane, made using only OO particles. EM density (0.04 contour) and ribbons are colored red and slate for each ABCD1 monomer, black sphere for R280, and green and yellow for modeled lipid-like entities and bound nucleotides, respectively. e Peroxisomal lumen with TMDs removed for clarity and f peroxisomal lumen with intracellular gate circled (dashed red line) with NBDs removed for clarity. TMs are numbered g electrostatic surface representation of ABCD1 viewed as a slice from the peroxisomal lumen.
