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| [[Image:1h6r.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1h6r| PDB=1h6r | SCENE= }} | | {{STRUCTURE_1h6r| PDB=1h6r | SCENE= }} |
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| '''THE OXIDIZED STATE OF A REDOX SENSITIVE VARIANT OF GREEN FLUORESCENT PROTEIN'''
| | ===THE OXIDIZED STATE OF A REDOX SENSITIVE VARIANT OF GREEN FLUORESCENT PROTEIN=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11689426}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11689426 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11689426}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Luminescence]] | | [[Category: Luminescence]] |
| [[Category: Yellow-emission]] | | [[Category: Yellow-emission]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:30:17 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:43:02 2008'' |
