8bmv
From Proteopedia
Ligand binding domain of the P. Putida receptor McpH in complex with Uric acid
Structural highlights
FunctionMCPH_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.[1] Publication Abstract from PubMedPurines 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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