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TitleMolecular mechanism of vectorial proton translocation by bacteriorhodopsin.
Journal, issue, pagesNature, Vol. 406, Issue 6796, Page 653-657, Year 2000
Publish dateAug 10, 2000
AuthorsS Subramaniam / R Henderson /
PubMed AbstractBacteriorhodopsin, a membrane protein with a relative molecular mass of 27,000, is a light driven pump which transports protons across the cell membrane of the halophilic organism Halobacterium ...Bacteriorhodopsin, a membrane protein with a relative molecular mass of 27,000, is a light driven pump which transports protons across the cell membrane of the halophilic organism Halobacterium salinarum. The chromophore retinal is covalently attached to the protein via a protonated Schiff base. Upon illumination, retinal is isomerized. The Schiff base then releases a proton to the extracellular medium, and is subsequently reprotonated from the cytoplasm. An atomic model for bacteriorhodopsin was first determined by Henderson et al, and has been confirmed and extended by work in a number of laboratories in the last few years. Here we present an atomic model for structural changes involved in the vectorial, light-driven transport of protons by bacteriorhodopsin. A 'switch' mechanism ensures the vectorial nature of pumping. First, retinal unbends, triggered by loss of the Schiff base proton, and second, a protein conformational change occurs. This conformational change, which we have determined by electron crystallography at atomic (3.2 A in-plane and 3.6 A vertical) resolution, is largely localized to helices F and G, and provides an 'opening' of the protein to protons on the cytoplasmic side of the membrane.
External linksNature / PubMed:10949309
MethodsEM (electron crystallography)
Resolution3.2 Å
Structure data

PDB-1fbb:
CRYSTAL STRUCTURE OF NATIVE CONFORMATION OF BACTERIORHODOPSIN
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 3.2 Å

PDB-1fbk:
CRYSTAL STRUCTURE OF CYTOPLASMICALLY OPEN CONFORMATION OF BACTERIORHODOPSIN
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 3.2 Å

Chemicals

ChemComp-RET:
RETINAL / Retinal

Source
  • halobacterium salinarum (Halophile)
KeywordsPROTON TRANSPORT / PROTON PUMP / MEMBRANE PROTEIN / RETINAL PROTEIN / TWO-DIMENSIONAL CRYSTAL ELECTRON DIFFRACTION / SINGLE CRYSTAL

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