8bmv

Ligand binding domain of the P. Putida receptor McpH in complex with Uric acid

spinqualitylabelsall models 8bmv, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8bmv is a 2 chain structure with sequence from Pseudomonas putida KT2440. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: URC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCPH_PSEPK Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpH is a chemoreceptor that binds and responds exclusively to intermediates of the purine degradation pathway. Publication Abstract from PubMed Purines and their derivatives control intracellular energy homeostasis and nucleotide synthesis, and act as signaling molecules. Here, we combine structural and sequence information to define a purine-binding motif that is present in sensor domains of thousands of bacterial receptors that modulate motility, gene expression, metabolism, and second-messenger turnover. Microcalorimetric titrations of selected sensor domains validate their ability to specifically bind purine derivatives, and evolutionary analyses indicate that purine sensors share a common ancestor with amino-acid receptors. Furthermore, we provide experimental evidence of physiological relevance of purine sensing in a second-messenger signaling system that modulates c-di-GMP levels. Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria.,Monteagudo-Cascales E, Gumerov VM, Fernandez M, Matilla MA, Gavira JA, Zhulin IB, Krell T Nat Commun. 2024 Jul 12;15(1):5867. doi: 10.1038/s41467-024-50275-3. PMID:38997289 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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