1b9c
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(New page: 200px<br /><applet load="1b9c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b9c, resolution 2.4Å" /> '''Green Fluorescent Pro...)
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Revision as of 09:21, 20 November 2007
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Green Fluorescent Protein Mutant F99S, M153T and V163A
Overview
The mutant F99S/M153T/V163A of the Green Fluorescent Protein (c3-GFP) has, spectral characteristics similar to the wild-type GFP, but it is 42-fold, more fluorescent in vivo. Here, we report the crystal structure and the, refolding properties of c3-GFP and compare them with those of the less, fluorescent wt-GFP and S65T mutant. The topology and the overall structure, of c3-GFP is similar to the wild-type GFP. The three mutated residues, Ser99, Thr153, and Ala163, lie on the surface of the protein in three, different beta-strands. The side chains of Ser99 and Thr153 are exposed to, the solvent, whereas that of Ala163 points toward the interior of the, protein. No significant deviation from the structure of the wild-type, molecule is found around these positions, and there is not clear evidence, of any distortion in the position of the chromophore or of the surrounding, residues induced by the mutated amino acids. In vitro refolding, experiments on urea-denatured c3-GFP reveal a renaturation behavior, similar to that of the S65T molecule, with kinetic constants of the same, order of magnitude. We conclude that the higher fluorescence activity of, c3-GFP can be attributed neither to particular structural features nor to, a faster folding process, as previously proposed.
About this Structure
1B9C is a Single protein structure of sequence from Aequorea victoria. Full crystallographic information is available from OCA.
Reference
Crystal structure and refolding properties of the mutant F99S/M153T/V163A of the green fluorescent protein., Battistutta R, Negro A, Zanotti G, Proteins. 2000 Dec 1;41(4):429-37. PMID:11056031
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