4r38

LOV domain from Erythrobacter litoralis EL346 blue-light activated histidine kinase

spinqualitylabelsall models 4r38, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4r38 is a 4 chain structure with sequence from Erythrobacter litoralis HTCC2594. The March 2015 RCSB PDB Molecule of the Month feature on Phototropin by David Goodsell is 10.2210/rcsb_pdb/mom_2015_3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: RBF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LVHK2_ERYLH Photosensitive kinase that is involved in increased bacterial virulence upon exposure to light. Publication Abstract from PubMed Although histidine kinases (HKs) are critical sensors of external stimuli in prokaryotes, the mechanisms by which their sensor domains control enzymatic activity remain unclear. Here, we report the full-length structure of a blue light-activated HK from Erythrobacter litoralis HTCC2594 (EL346) and the results of biochemical and biophysical studies that explain how it is activated by light. Contrary to the standard view that signaling occurs within HK dimers, EL346 functions as a monomer. Its structure reveals that the light-oxygen-voltage (LOV) sensor domain both controls kinase activity and prevents dimerization by binding one side of a dimerization/histidine phosphotransfer-like (DHpL) domain. The DHpL domain also contacts the catalytic/ATP-binding (CA) domain, keeping EL346 in an inhibited conformation in the dark. Upon light stimulation, interdomain interactions weaken to facilitate activation. Our data suggest that the LOV domain controls kinase activity by affecting the stability of the DHpL/CA interface, releasing the CA domain from an inhibited conformation upon photoactivation. We suggest parallels between EL346 and dimeric HKs, with sensor-induced movements in the DHp similarly remodeling the DHp/CA interface as part of activation. Full-length structure of a monomeric histidine kinase reveals basis for sensory regulation.,Rivera-Cancel G, Ko WH, Tomchick DR, Correa F, Gardner KH Proc Natl Acad Sci U S A. 2014 Dec 16;111(50):17839-44. doi:, 10.1073/pnas.1413983111. Epub 2014 Dec 2. PMID:25468971 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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