1bm1
From Proteopedia
(New page: 200px<br /><applet load="1bm1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bm1, resolution 3.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1bm1.gif|left|200px]]<br /><applet load="1bm1" size=" | + | [[Image:1bm1.gif|left|200px]]<br /><applet load="1bm1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bm1, resolution 3.5Å" /> | caption="1bm1, resolution 3.5Å" /> | ||
'''CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE'''<br /> | '''CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In the purple membrane of Halobacterium salinarium, bacteriorhodopsin | + | In the purple membrane of Halobacterium salinarium, bacteriorhodopsin trimers are arranged in a hexagonal lattice. When purple membrane sheets are incubated at high temperature with neutral detergent, membrane vesicularization takes place, yielding inside-out vesicles with a diameter of 50 nm. The vesicular structure becomes unstable at low temperature, where successive fusion of the vesicles yields a crystal which is composed of stacked planar membranes. X-ray crystallographic analysis reveals that the bacteriorhodopsin trimers are arranged in a honeycomb lattice in each membrane layer and that neighbouring membranes orient in opposite directions. The native structure of the trimeric unit is preserved in the honeycomb lattice, irrespective of alterations in the in-plane orientation of the trimer. One phospholipid tightly bound to a crevice between monomers in the trimeric unit is suggested to act as a glue in the formation of the trimer. |
==About this Structure== | ==About this Structure== | ||
| - | 1BM1 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 and DPG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1BM1 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 <scene name='pdbligand=RET:'>RET</scene> and <scene name='pdbligand=DPG:'>DPG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: retinal protein]] | [[Category: retinal protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:43 2008'' |
Revision as of 09:56, 21 February 2008
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CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE
Overview
In the purple membrane of Halobacterium salinarium, bacteriorhodopsin trimers are arranged in a hexagonal lattice. When purple membrane sheets are incubated at high temperature with neutral detergent, membrane vesicularization takes place, yielding inside-out vesicles with a diameter of 50 nm. The vesicular structure becomes unstable at low temperature, where successive fusion of the vesicles yields a crystal which is composed of stacked planar membranes. X-ray crystallographic analysis reveals that the bacteriorhodopsin trimers are arranged in a honeycomb lattice in each membrane layer and that neighbouring membranes orient in opposite directions. The native structure of the trimeric unit is preserved in the honeycomb lattice, irrespective of alterations in the in-plane orientation of the trimer. One phospholipid tightly bound to a crevice between monomers in the trimeric unit is suggested to act as a glue in the formation of the trimer.
About this Structure
1BM1 is a Single protein structure of sequence from Halobacterium salinarum with and as ligands. Full crystallographic information is available from OCA.
Reference
Specific lipid-protein interactions in a novel honeycomb lattice structure of bacteriorhodopsin., Sato H, Takeda K, Tani K, Hino T, Okada T, Nakasako M, Kamiya N, Kouyama T, Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1251-6. PMID:10393291
Page seeded by OCA on Thu Feb 21 11:56:43 2008
Categories: Halobacterium salinarum | Single protein | Hino, T. | Kamiya, N. | Kouyama, T. | Nakasako, M. | Okada, T. | Sato, H. | Takeda, K. | Tani, K. | DPG | RET | Membrane protein | Photoreceptor | Proton pump | Retinal protein
