5llw | pdb_00005llw

Bacteriophytochrome activated diguanylyl cyclase from Idiomarina species A28L

spinqualitylabelsall models 5llw, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5llw 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 3Å Ligands: CL, LBV, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F7RW09_9GAMM Publication Abstract from PubMed Nature has evolved an astonishingly modular architecture of covalently linked protein domains with diverse functionalities to enable complex cellular networks that are critical for cell survival. The coupling of sensory modules with enzymatic effectors allows direct allosteric regulation of cellular signaling molecules in response to diverse stimuli. We present molecular details of red light-sensing bacteriophytochromes linked to cyclic dimeric guanosine monophosphate-producing diguanylyl cyclases. Elucidation of the first crystal structure of a full-length phytochrome with its enzymatic effector, in combination with the characterization of light-induced changes in conformational dynamics, reveals how allosteric light regulation is fine-tuned by the architecture and composition of the coiled-coil sensor-effector linker and also the central helical spine. We anticipate that consideration of molecular principles of sensor-effector coupling, going beyond the length of the characteristic linker, and the appreciation of dynamically driven allostery will open up new directions for the design of novel red light-regulated optogenetic tools. Long-range allosteric signaling in red light-regulated diguanylyl cyclases.,Gourinchas G, Etzl S, Gobl C, Vide U, Madl T, Winkler A Sci Adv. 2017 Mar 3;3(3):e1602498. doi: 10.1126/sciadv.1602498. eCollection 2017 , Mar. PMID:28275738 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Diguanylate cyclase

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