1ggx

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(New page: 200px<br /><applet load="1ggx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ggx, resolution 1.90&Aring;" /> '''RED FLUORESCENT PROT...)
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[[Image:1ggx.gif|left|200px]]<br /><applet load="1ggx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ggx.gif|left|200px]]<br /><applet load="1ggx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ggx, resolution 1.90&Aring;" />
caption="1ggx, resolution 1.90&Aring;" />
'''RED FLUORESCENT PROTEIN (FP583 OR DSRED(CLONTECH)) FROM DISCOSOMA SP.'''<br />
'''RED FLUORESCENT PROTEIN (FP583 OR DSRED(CLONTECH)) FROM DISCOSOMA SP.'''<br />
==Overview==
==Overview==
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Green fluorescent protein (GFP) has rapidly become a standard tool for, investigating a variety of cellular activities, and has served as a model, system for understanding spectral tuning in chromophoric proteins. Distant, homologs of GFP in reef coral and anemone display two new properties of, the fluorescent protein family: dramatically red-shifted spectra, and, oligomerization to form tetramers. We now report the 1.9 A crystal, structure of DsRed, a red fluorescent protein from Discosoma coral. DsRed, monomers show similar topology to GFP, but additional chemical, modification to the chromophore extends the conjugated pi-system and, likely accounts for the red-shifted spectra. Oligomerization of DsRed, occurs at two chemically distinct protein interfaces to assemble the, tetramer. The DsRed structure reveals the chemical basis for the, functional properties of red fluorescent proteins and provides the basis, for rational engineering of this subfamily of GFP homologs.
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Green fluorescent protein (GFP) has rapidly become a standard tool for investigating a variety of cellular activities, and has served as a model system for understanding spectral tuning in chromophoric proteins. Distant homologs of GFP in reef coral and anemone display two new properties of the fluorescent protein family: dramatically red-shifted spectra, and oligomerization to form tetramers. We now report the 1.9 A crystal structure of DsRed, a red fluorescent protein from Discosoma coral. DsRed monomers show similar topology to GFP, but additional chemical modification to the chromophore extends the conjugated pi-system and likely accounts for the red-shifted spectra. Oligomerization of DsRed occurs at two chemically distinct protein interfaces to assemble the tetramer. The DsRed structure reveals the chemical basis for the functional properties of red fluorescent proteins and provides the basis for rational engineering of this subfamily of GFP homologs.
==About this Structure==
==About this Structure==
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1GGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Discosoma_sp. Discosoma sp.]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GGX OCA].
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1GGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Discosoma_sp. Discosoma sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GGX OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ranganathan, R.]]
[[Category: Ranganathan, R.]]
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[[Category: Socolich, M.A.]]
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[[Category: Socolich, M A.]]
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[[Category: Wall, M.A.]]
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[[Category: Wall, M A.]]
[[Category: chromophore]]
[[Category: chromophore]]
[[Category: fluorescent protein]]
[[Category: fluorescent protein]]
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[[Category: rfp]]
[[Category: rfp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:02:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:55 2008''

Revision as of 10:49, 21 February 2008


1ggx, resolution 1.90Å

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RED FLUORESCENT PROTEIN (FP583 OR DSRED(CLONTECH)) FROM DISCOSOMA SP.

Overview

Green fluorescent protein (GFP) has rapidly become a standard tool for investigating a variety of cellular activities, and has served as a model system for understanding spectral tuning in chromophoric proteins. Distant homologs of GFP in reef coral and anemone display two new properties of the fluorescent protein family: dramatically red-shifted spectra, and oligomerization to form tetramers. We now report the 1.9 A crystal structure of DsRed, a red fluorescent protein from Discosoma coral. DsRed monomers show similar topology to GFP, but additional chemical modification to the chromophore extends the conjugated pi-system and likely accounts for the red-shifted spectra. Oligomerization of DsRed occurs at two chemically distinct protein interfaces to assemble the tetramer. The DsRed structure reveals the chemical basis for the functional properties of red fluorescent proteins and provides the basis for rational engineering of this subfamily of GFP homologs.

About this Structure

1GGX is a Single protein structure of sequence from Discosoma sp.. Full crystallographic information is available from OCA.

Reference

The structural basis for red fluorescence in the tetrameric GFP homolog DsRed., Wall MA, Socolich M, Ranganathan R, Nat Struct Biol. 2000 Dec;7(12):1133-8. PMID:11101896

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