2a56: Difference between revisions

Revision as of 12:33, 29 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:2a56.png

Template:STRUCTURE 2a56

fluorescent protein asFP595, A143S, on-state, 5min irradiationfluorescent protein asFP595, A143S, on-state, 5min irradiation

Template:ABSTRACT PUBMED 16135569

About this StructureAbout this Structure

2A56 is a Protein complex structure of sequences from Anemonia sulcata. Full crystallographic information is available from OCA.

ReferenceReference

Structure and mechanism of the reversible photoswitch of a fluorescent protein., Andresen M, Wahl MC, Stiel AC, Grater F, Schafer LV, Trowitzsch S, Weber G, Eggeling C, Grubmuller H, Hell SW, Jakobs S, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13070-4. Epub 2005 Aug 31. PMID:16135569

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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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-'''fluorescent protein asFP595, A143S, on-state, 5min irradiation'''
+===fluorescent protein asFP595, A143S, on-state, 5min irradiation===
-==Overview==
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-Proteins that can be reversibly photoswitched between a fluorescent and a nonfluorescent state bear enormous potential in diverse fields, such as data storage, in vivo protein tracking, and subdiffraction resolution light microscopy. However, these proteins could hitherto not live up to their full potential because the molecular switching mechanism is not resolved. Here, we clarify the molecular photoswitching mechanism of asFP595, a green fluorescent protein (GFP)-like protein that can be transferred from a nonfluorescent "off" to a fluorescent "on" state and back again, by green and blue light, respectively. To this end, we establish reversible photoswitching of fluorescence in whole protein crystals and show that the switching kinetics in the crystal is identical with that in solution. Subsequent x-ray analysis demonstrated that upon the absorption of a green photon, the chromophore isomerizes from a trans (off) to a cis (on) state. Molecular dynamics calculations suggest that isomerization occurs through a bottom hula twist mechanism with concomitant rotation of both bonds of the chromophoric methine ring bridge. This insight into the switching mechanism should facilitate the targeted design of photoswitchable proteins. Reversible photoswitching of the protein chromophore system within intact crystals also constitutes a step toward the use of fluorescent proteins in three-dimensional data recording.
+The line below this paragraph, {{ABSTRACT_PUBMED_16135569}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Photochromic protein]]
 [[Category: Reversible photoswitch]]
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