6et7 | pdb_00006et7

Activated heterodimer of the bacteriophytochrome regulated diguanylyl cyclase variant - S505V A526V - from Idiomarina species A28L

spinqualitylabelsall models 6et7, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6et7 is a 2 chain structure with sequence from Idiomarina sp. A28L. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.852Å Ligands: CL, LBV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F7RW09_9GAMM Publication Abstract from PubMed Organisms adapt to environmental cues using diverse signaling networks. In order to sense and integrate light for regulating various biological functions, photoreceptor proteins have evolved in a modular way. This modularity is targeted in the development of optogenetic tools enabling the control of cellular events with high spatiotemporal precision. However, the limited understanding of signaling mechanisms impedes the rational design of innovative photoreceptor-effector couples. Here we reveal molecular details of signal transduction in phytochrome-regulated diguanylyl-cyclases. Asymmetric structural changes of the full-length homodimer result in a functional heterodimer featuring two different photoactivation states. Structural changes around the cofactors result in a quasi-translational rearrangement of the distant coiled-coil sensor-effector linker. Eventually, this regulates enzymatic activity by modulating the dimer interface of the output domains. Considering the importance of phytochrome heterodimerization in plant signaling, our mechanistic details of asymmetric photoactivation in a bacterial system reveal novel aspects of the evolutionary adaptation of phytochromes. Asymmetric activation mechanism of a homodimeric red light regulated photoreceptor.,Gourinchas G, Heintz U, Winkler A Elife. 2018 Jun 5;7. pii: 34815. doi: 10.7554/eLife.34815. PMID:29869984 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Diguanylate cyclase

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