X-ray crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane.

Cartailler JP, Luecke H
Annu Rev Biophys Biomol Struct. 2003 32: 285-310

PMID: 12598369 · DOI:10.1146/annurev.biophys.32.110601.142516

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.

MeSH Terms (11)

Bacteriorhodopsins Binding Sites Crystallography, X-Ray Macromolecular Substances Membrane Lipids Models, Molecular Molecular Conformation Motion Protein Binding Protein Conformation Purple Membrane

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