Extended Data Fig. 3: ForCE interaction with lipids.
From: A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases
a. Crystallographic and b. cryo-EM lipid composition inside the cavity formed by ForE tetramer. Structures are displayed in surface for the protein residues. Lipids, menaquinone and FeS clusters are depicted as sticks. ForC and ForE proteins surfaces are colored in dark blue and orange respectively. Non-protein carbon, oxygen, sulfur and iron atoms are colored in light blue, red, yellow and brown, respectively. c. Crystallographic and d. cryo-EM ForE central cavity access. ForC and ForE proteins surface are colored in dark blue and orange respectively. Glycero-phospholipid carbon, oxygen, and phosphorus atoms are colored in light blue, red and orange respectively. e. Hydrophobic (left) and electrostatic (center and right) surface calculations of the ForCE protein. Hydrophobic and hydrophilic residues are colored in light orange and light blue respectively. The cutaway shows the internal surface of ForE lined with hydrophobic residues (left). Positively charged amino acids are colored in blue, negatively charged amino acids in red, and neutral residues in white. The membrane was positioned at the level of the C-terminal end of the ForE tube capped by fatty acids (center). The right view shows the electrostatic potential of the HMP interacting with phospholipids.
