2c9i

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[[Image:2c9i.jpg|left|200px]]
[[Image:2c9i.jpg|left|200px]]
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{{Structure
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|PDB= 2c9i |SIZE=350|CAPTION= <scene name='initialview01'>2c9i</scene>, resolution 1.82&Aring;
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The line below this paragraph, containing "STRUCTURE_2c9i", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CRQ:[2-(3-CARBAMOYL-1-IMINO-PROPYL)-4-(4-HYDROXY-BENZYLIDENE)-5-OXO-4,5-DIHYDRO-IMIDAZOL-1-YL]-ACETIC+ACID'>CRQ</scene>
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{{STRUCTURE_2c9i| PDB=2c9i | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9i OCA], [http://www.ebi.ac.uk/pdbsum/2c9i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c9i RCSB]</span>
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'''STRUCTURE OF THE FLUORESCENT PROTEIN ASFP499 FROM ANEMONIA SULCATA'''
'''STRUCTURE OF THE FLUORESCENT PROTEIN ASFP499 FROM ANEMONIA SULCATA'''
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[[Category: Vallone, B.]]
[[Category: Vallone, B.]]
[[Category: Wiedenmann, J.]]
[[Category: Wiedenmann, J.]]
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[[Category: beta-barrel]]
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[[Category: Beta-barrel]]
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[[Category: bioluminescence]]
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[[Category: Bioluminescence]]
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[[Category: fluorescent protein]]
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[[Category: Fluorescent protein]]
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[[Category: luminescence]]
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[[Category: Luminescence]]
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[[Category: luminescent protein]]
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[[Category: Luminescent protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:30:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:18:26 2008''
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Revision as of 18:30, 3 May 2008

Image:2c9i.jpg

Template:STRUCTURE 2c9i

STRUCTURE OF THE FLUORESCENT PROTEIN ASFP499 FROM ANEMONIA SULCATA


Overview

Despite their similar fold topologies, anthozoan fluorescent proteins (FPs) can exhibit widely different optical properties, arising either from chemical modification of the chromophore itself or from specific interactions of the chromophore with the surrounding protein moiety. Here we present a structural and spectroscopic investigation of the green FP asFP499 from the sea anemone Anemonia sulcata var. rufescens to explore the effects of the protein environment on the chromophore. The optical absorption and fluorescence spectra reveal two discrete species populated in significant proportions over a wide pH range. Moreover, multiple protonation reactions are evident from the observed pH-dependent spectral changes. The x-ray structure of asFP499, determined by molecular replacement at a resolution of 1.85 A, shows the typical beta-barrel fold of the green FP from Aequorea victoria (avGFP). In its center, the chromophore, formed from the tripeptide Gln(63)-Tyr(64)-Gly(65), is tightly held by multiple hydrogen bonds in a polar cage that is structurally quite dissimilar to that of avGFP. The x-ray structure provides interesting clues as to how the spectroscopic properties are fine tuned by the chromophore environment.

About this Structure

2C9I is a Single protein structure of sequence from Anemonia sulcata. Full crystallographic information is available from OCA.

Reference

Chromophore-protein interactions in the anthozoan green fluorescent protein asFP499., Nienhaus K, Renzi F, Vallone B, Wiedenmann J, Nienhaus GU, Biophys J. 2006 Dec 1;91(11):4210-20. Epub 2006 Sep 15. PMID:16980366 Page seeded by OCA on Sat May 3 21:30:43 2008

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