2ote
From Proteopedia
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- | [[Image:2ote.jpg|left|200px]] | + | [[Image:2ote.jpg|left|200px]] |
- | + | ||
- | '''Crystal structure of a monomeric cyan fluorescent protein in the photobleached state''' | + | {{Structure |
+ | |PDB= 2ote |SIZE=350|CAPTION= <scene name='initialview01'>2ote</scene>, resolution 1.47Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= cFP484 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=86521 Clavularia sp.]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of a monomeric cyan fluorescent protein in the photobleached state''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2OTE is a [ | + | 2OTE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clavularia_sp. Clavularia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OTE OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17420458 17420458] |
[[Category: Clavularia sp.]] | [[Category: Clavularia sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: fluorescent protein]] | [[Category: fluorescent protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:04:17 2008'' |
Revision as of 16:04, 20 March 2008
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, resolution 1.47Å | |||||||
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Ligands: | |||||||
Gene: | cFP484 (Clavularia sp.) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of a monomeric cyan fluorescent protein in the photobleached 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
2OTE 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
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