1fbb
From Proteopedia
(New page: 200px<br /> <applet load="1fbb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fbb, resolution 3.2Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1fbb. | + | [[Image:1fbb.jpg|left|200px]]<br /><applet load="1fbb" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1fbb" size=" | + | |
caption="1fbb, resolution 3.2Å" /> | caption="1fbb, resolution 3.2Å" /> | ||
'''CRYSTAL STRUCTURE OF NATIVE CONFORMATION OF BACTERIORHODOPSIN'''<br /> | '''CRYSTAL STRUCTURE OF NATIVE CONFORMATION OF BACTERIORHODOPSIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FBB 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]. The following page contains interesting information on the relation of 1FBB with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb27_1.html Bacteriorhodopsin]]. Full crystallographic information is available from [http:// | + | 1FBB 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> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1FBB with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb27_1.html Bacteriorhodopsin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two-dimensional crystal electron diffraction]] | [[Category: two-dimensional crystal electron diffraction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:46:56 2008'' |
Revision as of 13:46, 15 February 2008
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CRYSTAL STRUCTURE OF NATIVE CONFORMATION OF BACTERIORHODOPSIN
Overview
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.
About this Structure
1FBB is a Single protein structure of sequence from Halobacterium salinarum with as ligand. The following page contains interesting information on the relation of 1FBB with [Bacteriorhodopsin]. Full crystallographic information is available from OCA.
Reference
Molecular mechanism of vectorial proton translocation by bacteriorhodopsin., Subramaniam S, Henderson R, Nature. 2000 Aug 10;406(6796):653-7. PMID:10949309
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