1h6r
From Proteopedia
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| - | [[Image:1h6r.gif|left|200px]] | + | [[Image:1h6r.gif|left|200px]] |
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| - | '''THE OXIDIZED STATE OF A REDOX SENSITIVE VARIANT OF GREEN FLUORESCENT PROTEIN''' | + | {{Structure |
| + | |PDB= 1h6r |SIZE=350|CAPTION= <scene name='initialview01'>1h6r</scene>, resolution 1.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE OXIDIZED STATE OF A REDOX SENSITIVE VARIANT OF GREEN FLUORESCENT PROTEIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H6R is a [ | + | 1H6R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6R OCA]. |
==Reference== | ==Reference== | ||
| - | Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein., Ostergaard H, Henriksen A, Hansen FG, Winther JR, EMBO J. 2001 Nov 1;20(21):5853-62. PMID:[http:// | + | Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein., Ostergaard H, Henriksen A, Hansen FG, Winther JR, EMBO J. 2001 Nov 1;20(21):5853-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11689426 11689426] |
[[Category: Aequorea victoria]] | [[Category: Aequorea victoria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: yellow-emission]] | [[Category: yellow-emission]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:33:00 2008'' |
Revision as of 09:33, 20 March 2008
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| , resolution 1.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE OXIDIZED STATE OF A REDOX SENSITIVE VARIANT OF GREEN FLUORESCENT PROTEIN
Overview
To visualize the formation of disulfide bonds in living cells, a pair of redox-active cysteines was introduced into the yellow fluorescent variant of green fluorescent protein. Formation of a disulfide bond between the two cysteines was fully reversible and resulted in a >2-fold decrease in the intrinsic fluorescence. Inter conversion between the two redox states could thus be followed in vitro as well as in vivo by non-invasive fluorimetric measurements. The 1.5 A crystal structure of the oxidized protein revealed a disulfide bond-induced distortion of the beta-barrel, as well as a structural reorganization of residues in the immediate chromophore environment. By combining this information with spectroscopic data, we propose a detailed mechanism accounting for the observed redox state-dependent fluorescence. The redox potential of the cysteine couple was found to be within the physiological range for redox-active cysteines. In the cytoplasm of Escherichia coli, the protein was a sensitive probe for the redox changes that occur upon disruption of the thioredoxin reductive pathway.
About this Structure
1H6R is a Single protein structure of sequence from Aequorea victoria. Full crystallographic information is available from OCA.
Reference
Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein., Ostergaard H, Henriksen A, Hansen FG, Winther JR, EMBO J. 2001 Nov 1;20(21):5853-62. PMID:11689426
Page seeded by OCA on Thu Mar 20 11:33:00 2008
