1h6r
From Proteopedia
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|PDB= 1h6r |SIZE=350|CAPTION= <scene name='initialview01'>1h6r</scene>, resolution 1.50Å | |PDB= 1h6r |SIZE=350|CAPTION= <scene name='initialview01'>1h6r</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Ostergaard, H.]] | [[Category: Ostergaard, H.]] | ||
[[Category: Winther, J R.]] | [[Category: Winther, J R.]] | ||
| - | [[Category: CL]] | ||
[[Category: green fluorescent protein]] | [[Category: green fluorescent protein]] | ||
[[Category: luminescence]] | [[Category: luminescence]] | ||
[[Category: yellow-emission]] | [[Category: yellow-emission]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:53 2008'' |
Revision as of 17:58, 30 March 2008
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| , resolution 1.50Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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