Structural Details of an Interaction between Cardiolipin and an Integral Membrane Protein

• Published in: Proceedings of the National Academy of Sciences - PNAS 1999-12, Vol.96 (26), p.14706-14711
• Main Authors: McAuley, Katherine E., Fyfe, Paul K., Ridge, Justin P., Isaacs, Neil W., Cogdell, Richard J., Jones, Michael R.
• Format: Article
• Language: English
• Subjects: Atoms; Binding Sites; Biochemistry; Biological Sciences; cardiolipin; Cardiolipins; Cardiolipins - chemistry; Cardiolipins - metabolism; Crystallography, X-Ray; Crystals; Electron density; Lipids; Membrane proteins; Membranes; Models, Molecular; Molecular structure; Molecules; P branes; Photosynthetic Reaction Center Complex Proteins - chemistry; Photosynthetic Reaction Center Complex Proteins - genetics; Photosynthetic Reaction Center Complex Proteins - metabolism; Protein Structure, Tertiary; Proteins; Rhodobacter sphaeroides - chemistry; Rhodobacter sphaeroides - genetics
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.96.26.14706

Anionic lipids play a variety of key roles in biomembrane function, including providing the immediate environment for the integral membrane proteins that catalyze photosynthetic and respiratory energy transduction. Little is known about the molecular basis of these lipid-protein interactions. In this study, x-ray crystallography has been used to examine the structural details of an interaction between cardiolipin and the photoreaction center, a key light-driven electron transfer protein complex found in the cytoplasmic membrane of photosynthetic bacteria. X-ray diffraction data collected over the resolution range 30.0-2.1 angstrom show that binding of the lipid to the protein involves a combination of ionic interactions between the protein and the lipid headgroup and van der Waals interactions between the lipid tails and the electroneutral intramembrane surface of the protein. In the headgroup region, ionic interactions involve polar groups of a number of residues, the protein backbone, and bound water molecules. The lipid tails sit along largely hydrophobic grooves in the irregular surface of the protein. In addition to providing new information on the immediate lipid environment of a key integral membrane protein, this study provides the first, to our knowledge, high-resolution x-ray crystal structure for cardiolipin. The possible significance of this interaction between an integral membrane protein and cardiolipin is considered.