1h6r

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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'''
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===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 &gt;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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11689426 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11689426}}
==About this Structure==
==About this Structure==
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[[Category: Luminescence]]
[[Category: Luminescence]]
[[Category: Yellow-emission]]
[[Category: Yellow-emission]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:30:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:43:02 2008''

Revision as of 03:43, 1 July 2008

Template:STRUCTURE 1h6r

THE OXIDIZED STATE OF A REDOX SENSITIVE VARIANT OF GREEN FLUORESCENT PROTEIN

Template:ABSTRACT PUBMED 11689426

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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