2ie2

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(New page: 200px<br /><applet load="2ie2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ie2, resolution 1.70&Aring;" /> '''The 1.7 A crystal st...)
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==Overview==
==Overview==
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The green fluorescent protein (GFP), its variants, and the closely related, GFP-like proteins possess a wide variety of spectral properties that are, of widespread interest as biological tools. One desirable spectral, property, termed photoswitching, involves the light-induced alteration of, the optical properties of certain GFP members. Although the structural, basis of both reversible and irreversible photoswitching events have begun, to be unraveled, the mechanisms resulting in reversible photoswitching are, less clear. A novel GFP-like protein, Dronpa, was identified to have, remarkable light-induced photoswitching properties, maintaining an almost, perfect reversible photochromic behavior with a high fluorescence to dark, state ratio. We have crystallized and subsequently determined to 1.7 A, resolution the crystal structure of the fluorescent state of Dronpa. The, chromophore was observed to be in its anionic form, adopting a cis, co-planar conformation. Comparative structural analysis of, non-photoactivatable and photoactivatable GFPs, together with, site-directed mutagenesis of a position (Cys62) within the Dronpa, chromophore, has provided a basis for understanding Dronpa, photoactivation. Specifically, we propose a model of reversible, photoactivation whereby irradiation with light leads to subtle, conformational changes within and around the environment of the, chromophore that promotes proton transfer along an intricate polar, network.
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The green fluorescent protein (GFP), its variants, and the closely related GFP-like proteins possess a wide variety of spectral properties that are of widespread interest as biological tools. One desirable spectral property, termed photoswitching, involves the light-induced alteration of the optical properties of certain GFP members. Although the structural basis of both reversible and irreversible photoswitching events have begun to be unraveled, the mechanisms resulting in reversible photoswitching are less clear. A novel GFP-like protein, Dronpa, was identified to have remarkable light-induced photoswitching properties, maintaining an almost perfect reversible photochromic behavior with a high fluorescence to dark state ratio. We have crystallized and subsequently determined to 1.7 A resolution the crystal structure of the fluorescent state of Dronpa. The chromophore was observed to be in its anionic form, adopting a cis co-planar conformation. Comparative structural analysis of non-photoactivatable and photoactivatable GFPs, together with site-directed mutagenesis of a position (Cys62) within the Dronpa chromophore, has provided a basis for understanding Dronpa photoactivation. Specifically, we propose a model of reversible photoactivation whereby irradiation with light leads to subtle conformational changes within and around the environment of the chromophore that promotes proton transfer along an intricate polar network.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn, J.]]
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[[Category: Wilmann, P.G.]]
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[[Category: Wilmann, P G.]]
[[Category: beta barrel]]
[[Category: beta barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:39:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:43 2008''

Revision as of 15:51, 21 February 2008

Image:2ie2.gif

2ie2, resolution 1.70Å

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The 1.7 A crystal structure of Dronpa: a photoswitchable green fluorescent protein

Overview

The green fluorescent protein (GFP), its variants, and the closely related GFP-like proteins possess a wide variety of spectral properties that are of widespread interest as biological tools. One desirable spectral property, termed photoswitching, involves the light-induced alteration of the optical properties of certain GFP members. Although the structural basis of both reversible and irreversible photoswitching events have begun to be unraveled, the mechanisms resulting in reversible photoswitching are less clear. A novel GFP-like protein, Dronpa, was identified to have remarkable light-induced photoswitching properties, maintaining an almost perfect reversible photochromic behavior with a high fluorescence to dark state ratio. We have crystallized and subsequently determined to 1.7 A resolution the crystal structure of the fluorescent state of Dronpa. The chromophore was observed to be in its anionic form, adopting a cis co-planar conformation. Comparative structural analysis of non-photoactivatable and photoactivatable GFPs, together with site-directed mutagenesis of a position (Cys62) within the Dronpa chromophore, has provided a basis for understanding Dronpa photoactivation. Specifically, we propose a model of reversible photoactivation whereby irradiation with light leads to subtle conformational changes within and around the environment of the chromophore that promotes proton transfer along an intricate polar network.

About this Structure

2IE2 is a Single protein structure of sequence from Echinophyllia sp. sc22. Full crystallographic information is available from OCA.

Reference

The 1.7 A crystal structure of Dronpa: a photoswitchable green fluorescent protein., Wilmann PG, Turcic K, Battad JM, Wilce MC, Devenish RJ, Prescott M, Rossjohn J, J Mol Biol. 2006 Nov 24;364(2):213-24. Epub 2006 Sep 3. PMID:17010376

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