1h6r

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[[Image:1h6r.gif|left|200px]]
[[Image:1h6r.gif|left|200px]]
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{{Structure
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|PDB= 1h6r |SIZE=350|CAPTION= <scene name='initialview01'>1h6r</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1h6r", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PIA:{2-(1-AMINOETHYL)-4-[(4-HYDROXYPHENYL)METHYL]-5-OXO-2,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETALDEHYDE'>PIA</scene>
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{{STRUCTURE_1h6r| PDB=1h6r | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6r OCA], [http://www.ebi.ac.uk/pdbsum/1h6r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h6r RCSB]</span>
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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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[[Category: Ostergaard, H.]]
[[Category: Ostergaard, H.]]
[[Category: Winther, J R.]]
[[Category: Winther, J R.]]
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[[Category: green fluorescent protein]]
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[[Category: Green fluorescent protein]]
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[[Category: luminescence]]
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[[Category: Luminescence]]
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[[Category: yellow-emission]]
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[[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 Sun Mar 30 20:58:53 2008''
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Revision as of 15:30, 2 May 2008

Image:1h6r.gif

Template:STRUCTURE 1h6r

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 Fri May 2 18:30:17 2008

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