X-ray crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane.
The past decade has witnessed increasingly detailed insights into the structural mechanism of the bacteriorhodopsin photocycle. Concurrently, there has been much progress within our knowledge pertaining to the lipids of the purple membrane, including the discovery of new lipids and the overall effort to localize and identify each lipid within the purple membrane. Therefore, there is a need to classify this information to generalize the findings. We discuss the properties and roles of haloarchaeal lipids and present the structural data as individual case studies. Lipid-protein interactions are discussed in the context of structure-function relationships. A brief discussion of the possibility that bacteriorhodopsin functions as a light-driven inward hydroxide pump rather than an outward proton pump is also presented.
Cartailler
Jean-Philippe
JP
Department of Molecular Biology and Biochemistry, University of California Irvine, Irvine, California 92697-3900, USA.
Luecke
Hartmut
H
D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods*; D046911:Macromolecular Substances; D008563:Membrane Lipids / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D009038:Motion; D011485:Protein Binding; D011487:Protein Conformation; D018717:Purple Membrane / Q000737:chemistry* / Q000378:metabolism
D046911:Macromolecular Substances; D008563:Membrane Lipids; D001436:Bacteriorhodopsins