1ap9
From Proteopedia
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| - | [[Image:1ap9.gif|left|200px]]<br /> | + | [[Image:1ap9.gif|left|200px]]<br /><applet load="1ap9" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ap9" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ap9, resolution 2.35Å" /> | caption="1ap9, resolution 2.35Å" /> | ||
'''X-RAY STRUCTURE OF BACTERIORHODOPSIN FROM MICROCRYSTALS GROWN IN LIPIDIC CUBIC PHASES'''<br /> | '''X-RAY STRUCTURE OF BACTERIORHODOPSIN FROM MICROCRYSTALS GROWN IN LIPIDIC CUBIC PHASES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AP9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with RET as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1AP9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with RET as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=SFF:Schiff Base'>SFF</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AP9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: retinal protein]] | [[Category: retinal protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:19:19 2007'' |
Revision as of 12:09, 18 December 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. Known structural/functional Site: . 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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