5dkl

Structure of the light-state dimer of the blue light photoreceptor Aureochrome 1a LOV from P. tricornutum

spinqualitylabelsall models 5dkl, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dkl is a 2 chain structure with sequence from Phaeodactylum tricornutum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: FMN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7G9J2_PHATC Publication Abstract from PubMed The design of synthetic optogenetic tools that allow precise spatiotemporal control of biological processes previously inaccessible to optogenetic control has developed rapidly over the last years. Rational design of such tools requires detailed knowledge of allosteric light signaling in natural photoreceptors. To understand allosteric communication between sensor and effector domains, characterization of all relevant signaling states is required. Here, we describe the mechanism of light-dependent DNA binding of the light-oxygen-voltage (LOV) transcription factor Aureochrome 1a from Phaeodactylum tricornutum (PtAu1a) and present crystal structures of a dark state LOV monomer and a fully light-adapted LOV dimer. In combination with hydrogen/deuterium-exchange, solution scattering data and DNA-binding experiments, our studies reveal a light-sensitive interaction between the LOV and basic region leucine zipper DNA-binding domain that together with LOV dimerization results in modulation of the DNA affinity of PtAu1a. We discuss the implications of these results for the design of synthetic LOV-based photosensors with application in optogenetics. Blue light-induced LOV domain dimerization enhances the affinity of Aureochrome 1a for its target DNA sequence.,Heintz U, Schlichting I Elife. 2016 Jan 12;5:e11860. doi: 10.7554/eLife.11860. PMID:26754770 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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