2otb
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Fluorescent protein (FP) variants that can be reversibly converted between | + | Fluorescent protein (FP) variants that can be reversibly converted between fluorescent and nonfluorescent states have proven to be a catalyst for innovation in the field of fluorescence microscopy. However, the structural basis of the process remains poorly understood. High-resolution structures of a FP derived from Clavularia in both the fluorescent and the light-induced nonfluorescent states reveal that the rapid and complete loss of fluorescence observed upon illumination with 450-nm light results from cis-trans isomerization of the chromophore. The photoinduced change in configuration from the well ordered cis isomer to the highly nonplanar and disordered trans isomer is accompanied by a dramatic rearrangement of internal side chains. Taken together, the structures provide an explanation for the loss of fluorescence upon illumination, the slow light-independent recovery, and the rapid light-induced recovery of fluorescence. The fundamental mechanism appears to be common to all of the photoactivatable and reversibly photoswitchable FPs reported to date. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ai, H.]] | [[Category: Ai, H.]] | ||
| - | [[Category: Campbell, R | + | [[Category: Campbell, R E.]] |
| - | [[Category: Henderson, J | + | [[Category: Henderson, J N.]] |
| - | [[Category: Remington, S | + | [[Category: Remington, S J.]] |
[[Category: beta can]] | [[Category: beta can]] | ||
[[Category: fluorescent protein]] | [[Category: fluorescent protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:22:19 2008'' |
Revision as of 16:22, 21 February 2008
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Crystal structure of a monomeric cyan fluorescent protein in the fluorescent state
Overview
Fluorescent protein (FP) variants that can be reversibly converted between fluorescent and nonfluorescent states have proven to be a catalyst for innovation in the field of fluorescence microscopy. However, the structural basis of the process remains poorly understood. High-resolution structures of a FP derived from Clavularia in both the fluorescent and the light-induced nonfluorescent states reveal that the rapid and complete loss of fluorescence observed upon illumination with 450-nm light results from cis-trans isomerization of the chromophore. The photoinduced change in configuration from the well ordered cis isomer to the highly nonplanar and disordered trans isomer is accompanied by a dramatic rearrangement of internal side chains. Taken together, the structures provide an explanation for the loss of fluorescence upon illumination, the slow light-independent recovery, and the rapid light-induced recovery of fluorescence. The fundamental mechanism appears to be common to all of the photoactivatable and reversibly photoswitchable FPs reported to date.
About this Structure
2OTB is a Single protein structure of sequence from Clavularia sp.. Full crystallographic information is available from OCA.
Reference
Structural basis for reversible photobleaching of a green fluorescent protein homologue., Henderson JN, Ai HW, Campbell RE, Remington SJ, Proc Natl Acad Sci U S A. 2007 Apr 17;104(16):6672-7. Epub 2007 Apr 9. PMID:17420458
Page seeded by OCA on Thu Feb 21 18:22:19 2008
