1h6r: Difference between revisions
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[[Image:1h6r.gif|left|200px]] | [[Image:1h6r.gif|left|200px]] | ||
'''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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| 1h6r, resolution 1.50Å | |||||||||||||
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| Ligands: | CL | ||||||||||||
| 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
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