1ap9
From Proteopedia
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Revision as of 12:45, 30 October 2007
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X-RAY STRUCTURE OF BACTERIORHODOPSIN FROM MICROCRYSTALS GROWN IN LIPIDIC CUBIC PHASES
Overview
Lipidic cubic phases provide a continuous three-dimensional bilayer matrix, that facilitates nucleation and growth of bacteriorhodopsin microcrystals., The crystals diffract x-rays isotropically to 2.0 angstroms. The structure, of this light-driven proton pump was solved at a resolution of 2.5, angstroms by molecular replacement, using previous results from electron, crystallographic studies as a model. The earlier structure was generally, confirmed, but several differences were found, including loop, conformations and side chain residues. Eight water molecules are now, identified experimentally in the proton pathway. These findings reveal the, constituents of the proton translocation pathway in the ground state.
About this Structure
1AP9 is a [Single protein] structure of sequence from [Halobacterium salinarum] with RET as [ligand]. Structure known Active Site: SFF. Full crystallographic information is available from [OCA].
Reference
X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases., Pebay-Peyroula E, Rummel G, Rosenbusch JP, Landau EM, Science. 1997 Sep 12;277(5332):1676-81. PMID:9287223
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