2ote
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2ote |SIZE=350|CAPTION= <scene name='initialview01'>2ote</scene>, resolution 1.47Å | |PDB= 2ote |SIZE=350|CAPTION= <scene name='initialview01'>2ote</scene>, resolution 1.47Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AYG:[(4E)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>AYG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= cFP484 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=86521 Clavularia sp.]) | |GENE= cFP484 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=86521 Clavularia sp.]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2otb|2OTB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ote FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ote OCA], [http://www.ebi.ac.uk/pdbsum/2ote PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ote RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Henderson, J N.]] | [[Category: Henderson, J N.]] | ||
[[Category: Remington, S J.]] | [[Category: Remington, S J.]] | ||
| - | [[Category: ACT]] | ||
[[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 Mon Mar 31 04:22:49 2008'' |
Revision as of 01:22, 31 March 2008
| |||||||
| , resolution 1.47Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | cFP484 (Clavularia sp.) | ||||||
| Related: | 2OTB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 04:22:49 2008
