8BMV
Ligand binding domain of the P. Putida receptor McpH in complex with Uric acid
Summary for 8BMV
| Entry DOI | 10.2210/pdb8bmv/pdb |
| Descriptor | Methyl-accepting chemotaxis protein McpH, URIC ACID (3 entities in total) |
| Functional Keywords | ligand binding domain, chemoreceptor, pseudomonas putida, chemotactic transducer, signaling protein |
| Biological source | Pseudomonas putida KT2440 |
| Total number of polymer chains | 2 |
| Total formula weight | 61566.95 |
| Authors | Gavira, J.A.,Krell, T.,Fernandez, M.,Martinez-Rodriguez, S. (deposition date: 2022-11-11, release date: 2024-07-24) |
| Primary citation | Monteagudo-Cascales, E.,Gumerov, V.M.,Fernandez, M.,Matilla, M.A.,Gavira, J.A.,Zhulin, I.B.,Krell, T. Ubiquitous purine sensor modulates diverse signal transduction pathways in bacteria. Nat Commun, 15:5867-5867, 2024 Cited by PubMed Abstract: 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. PubMed: 38997289DOI: 10.1038/s41467-024-50275-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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