2wis

Fluorescent protein KillerRed in the bleached state

spinqualitylabelsall models 2wis, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wis is a 2 chain structure with sequence from Anthomedusae sp. DC-2005. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: CRQ, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2TCH5_9CNID Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The red fluorescent protein KillerRed, engineered from the hydrozoan chromoprotein anm2CP, has been reported to induce strong cytotoxicity through the chromophore assisted light inactivation (CALI) effect. Here, we present the X-ray structures of KillerRed in its native and bleached states. A long water-filled channel is revealed, connecting the methylene bridge of the chromophore to the solvent. This channel facilitates the transit of oxygen and of reactive oxygen species (ROS) formed by reaction with the excited chromophore. The functional roles of key mutations used to produce KillerRed are discussed, strong chromophore distortions in the bleached state are revealed, and mechanisms for ROS production and self protection are proposed. The presence of a partially mature, photo-resistant, green-emitting state is characterized, which accounts for enhanced CALI by "pre-bleached" KillerRed. Structural basis for the phototoxicity of the fluorescent protein KillerRed.,Carpentier P, Violot S, Blanchoin L, Bourgeois D FEBS Lett. 2009 Sep 3;583(17):2839-42. Epub 2009 Jul 30. PMID:19646983 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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