Fig. 1: Cryo-EM structures of glycerophospholipid transporter complex MlaFEDB from A. baumannii.
From: Cryo-EM structures of Acinetobacter baumannii glycerophospholipid transporter
a Cryo-EM structure of the MlaFEDB complex. MlaD, MlaE, MlaF and MlaB are colored separately. b The ATPase activities of MlaFEDB from A. baumannii and E. coli. Each point represents mean ± SD. c Overlay of the MCE domain of MlaD (left) and TMs of MlaED between A. baumannii (color) and E. coli (gray, PDB 7CGE). d Cross-sectional view (left) and periplasmic view (middle) of the model with phospholipid binding. Twelve glycerophospholipids (PLs) are modeled and are shown as stars in the cartoon view (right). Two PLs bound in the central cavity are colored red. PL1–3, PL4, and PL5 bound in one side cavity are shown and colored green, orange, and yellow, respectively. e Electrostatic surface view of the interaction between PL1–3 and MlaE, indicating areas of positive charge (blue). f Surface overlay of the MCE domain of MlaD between the nucleotide-free (gray) and Vtrans1, Vtrans2, and Vclose conformations. The arrows indicate the movement of MCE. g Cryo-EM densities for the nucleotides bound at the ATP-binding sites of two subunits of MlaF in Vtrans1 (raspberry), Vtrans2 (green), and Vclose (blue). ATP or ADP-VO4 binds to the Walker A and Signature motifs. R23, R26, K52, T53, T54, and E175 participate in the binding. h Structure overlay of MlaE in the nucleotide-free (gray) and Vclose (blue) conformations. Blue arrow indicates the movement of TMD of MlaE.
