title: Structural determinants of purple membrane assembly.
abstract: The purple membrane is a two-dimensional crystalline lattice formed by bacteriorhodopsin and lipid molecules in the cytoplasmic membrane of Halobacterium salinarum. High-resolution structural studies, in conjunction with detailed knowledge of the lipid composition, make the purple membrane one of the best models for elucidating the forces that are responsible for the assembly and stability of integral membrane protein complexes. In this review, recent mutational efforts to identify the structural features of bacteriorhodopsin that determine its assembly in the purple membrane are discussed in the context of structural, calorimetric and reconstitution studies. Quantitative evidence is presented that interactions between transmembrane helices of neighboring bacteriorhodopsin molecules contribute to purple membrane assembly. However, other specific interactions, particularly between bacteriorhodopsin and lipid molecules, may provide the major driving force for assembly. Elucidating the molecular basis of protein-protein and protein-lipid interactions in the purple membrane may provide insights into the formation of integral membrane protein complexes in other systems.
authors.affiliation: Department of Biomolecular Chemistry, University of Wisconsin Medical School, 53706-1532, Madison, WI, USA. mpkrebs@facstaff.wisc.edu
authors.forename: M P
authors.initials: MP
authors.lastname: Krebs
authors.forename: T A
authors.initials: TA
authors.lastname: Isenbarger
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry*; D006217:Halobacterium; D008051:Lipid Bilayers / Q000737:chemistry*; D008055:Lipids / Q000737:chemistry; D015394:Molecular Structure; D018717:Purple Membrane / Q000737:chemistry* / Q000648:ultrastructure; D013816:Thermodynamics
chemical_list: D008051:Lipid Bilayers; D008055:Lipids; D001436:Bacteriorhodopsins