2ie2: Difference between revisions

Revision as of 23:08, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ie2.png

Template:STRUCTURE 2ie2

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

Template:ABSTRACT PUBMED 17010376

About this StructureAbout this Structure

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

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The 1.7 A crystal structure of Dronpa: a photoswitchable green fluorescent protein'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17010376}}, adds the Publication Abstract to the page
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 ==About this Structure==
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