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The Directed Cooperative Assembly of Proteorhodopsin into 2D and 3D Polarized Arrays

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Specialty Science
Date 2007 May 10
PMID 17488827
Citations 10
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Abstract

Proteorhodopsin is the membrane protein used by marine bacterioplankton as a light-driven proton pump. Here, we describe a rapid cooperative assembly process directed by universal electrostatic interactions that spontaneously organizes proteorhodopsin molecules into ordered arrays with well defined orientation and packing density. We demonstrate the charge density-matching mechanism that selectively controls the assembly process. The interactions among different components in the system are tuned by varying their charge densities to yield different organized transmembrane protein arrays: (i) a bacteriorhodopsin purple membrane-like structure where proteorhodopsin molecules are cooperatively arranged with charged lipids into a 2D hexagonal lattice; (ii) selected liquid-crystalline states in which crystalline lamellae made up of the coassembled proteorhodopsin and charged lipid molecules are coupled three-dimensionally with polarized proteorhodopsin orientation persisting through the macroscopic scale. Understanding this rapid electrostatically driven assembly process sheds light on organizing membrane proteins in general, which is a prerequisite for membrane protein structural and mechanistic studies as well as in vitro applications.

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