2Z6Z

Crystal structure of a photoswitchable GFP-like protein Dronpa in the bright-state

Summary for 2Z6Z

• Entry DOI: 10.2210/pdb2z6z/pdb
• Related: 2Z1O 2Z6X 2Z6Y
• Descriptor: Fluorescent protein Dronpa (2 entities in total)
• Functional Keywords: gfp-like protein, photochromism, fluorescent protein
• Biological source: Echinophyllia sp. SC22
• Total number of polymer chains: 6
• Total formula weight: 175481.78

Authors

Kikuchi, A.,Jeyakanthan, J.,Taka, J.,Shiro, Y.,Mizuno, H.,Miyawaki, A. (deposition date: 2007-08-09, release date: 2008-07-22, Last modification date: 2024-10-23)

Primary citation

Mizuno, H.,Mal, T.K.,Walchli, M.,Kikuchi, A.,Fukano, T.,Ando, R.,Jeyakanthan, J.,Taka, J.,Shiro, Y.,Ikura, M.,Miyawaki, A.
Light-dependent regulation of structural flexibility in a photochromic fluorescent protein.
Proc.Natl.Acad.Sci.Usa, 105:9227-9232, 2008

PubMed Abstract: The structural basis for the photochromism in the fluorescent protein Dronpa is poorly understood, because the crystal structures of the bright state of the protein did not provide an answer to the mechanism of the photochromism, and structural determination of the dark state has been elusive. We performed NMR analyses of Dronpa in solution at ambient temperatures to find structural flexibility of the protein in the dark state. Light-induced changes in interactions between the chromophore and beta-barrel are responsible for switching between the two states. In the bright state, the apex of the chromophore tethers to the barrel by a hydrogen bond, and an imidazole ring protruding from the barrel stabilizes the plane of the chromophore. These interactions are disrupted by strong illumination with blue light, and the chromophore, together with a part of the beta-barrel, becomes flexible, leading to a nonradiative decay process.

PubMed: 18574155
DOI: 10.1073/pnas.0709599105

Experimental method

X-RAY DIFFRACTION (1.8 Å)