Fig. 2 Cardiolipin binding sites in complex I.

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Fig. 2 Cardiolipin binding sites in complex I. Cardiolipin binding sites in complex I. (A) Top: Cardiolipin (CDL) binding sites identified by CG-MD simulations of complex I from Thermus thermophilus. Bottom: Experimentally refined CDL molecules around cryo-EM structures of complex I from Ovis aries (6) (PDB ID: 5LNK) and Mus musculus (7) (PDB ID: 6G2J). Note that TM helices 1 to 3 of subunit Nqo14 (subunit in yellow, T. thermophilus) are not present in the homologous mammalian ND2 subunits. Both enzymes are viewed from the N-side of the membrane. The supernumerary subunits are omitted for visual clarity. (B) Statistics of lipid contacts with the membrane domain of complex I obtained from CG-MD simulations. (C) Autocorrelation function of the lipid binding dynamics. The average retention time for CDL is about six times higher than that for POPE or POPC, and ca. 12 times higher than that for Nqo8-bound CDL. (D) Top: Membrane-exposed phenylalanine residues in Nqo8. Bottom: Electrostatic potential map of complex I (front view). The color scale ranges from +10 kBT/e (blue, ca. +260 mV) to −10 kBT/e (red, ca. −260 mV). (E) Putative CDL binding sites in Nqo8, obtained from atomistic simulations, highlighting interactions with Arg37, Arg41, and phenylalanine residues. Alexander Jussupow et al. Sci Adv 2019;5:eaav1850 Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).