1bm1: Difference between revisions

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[[Image:1bm1.gif|left|200px]]<br /><applet load="1bm1" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1bm1.gif|left|200px]]
caption="1bm1, resolution 3.5&Aring;" />
 
'''CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE'''<br />
{{Structure
|PDB= 1bm1 |SIZE=350|CAPTION= <scene name='initialview01'>1bm1</scene>, resolution 3.5&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=RET:RETINAL'>RET</scene> and <scene name='pdbligand=DPG:PHOSPHORIC ACID 2,3-BIS-(3,7,11,15-TETRAMETHYL-HEXADECYLOXY)-PROPYL ESTER 2-HYDROXO-3-PHOSPHONOOXY-PROPYL ESTER'>DPG</scene>
|ACTIVITY=
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE'''
 


==Overview==
==Overview==
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==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 <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].  
1BM1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM1 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10393291 10393291]
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:[http://www.ncbi.nlm.nih.gov/pubmed/10393291 10393291]
[[Category: Halobacterium salinarum]]
[[Category: Halobacterium salinarum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: retinal protein]]
[[Category: retinal protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:43 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:52 2008''

Revision as of 11:12, 20 March 2008

File:1bm1.gif


PDB ID 1bm1

Drag the structure with the mouse to rotate
, resolution 3.5Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE


OverviewOverview

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 StructureAbout this Structure

1BM1 is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.

ReferenceReference

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

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