8bmv
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Ligand binding domain of the P. Putida receptor McpH in complex with Uric acid== | |
| + | <StructureSection load='8bmv' size='340' side='right'caption='[[8bmv]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8bmv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_KT2440 Pseudomonas putida KT2440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BMV FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=URC:URIC+ACID'>URC</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bmv OCA], [https://pdbe.org/8bmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bmv RCSB], [https://www.ebi.ac.uk/pdbsum/8bmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bmv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MCPH_PSEPK 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.<ref>PMID:26355499</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:38997289</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8bmv" style="background-color:#fffaf0;"></div> |
| - | [[Category: Fernandez | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas putida KT2440]] | ||
| + | [[Category: Fernandez M]] | ||
| + | [[Category: Gavira JA]] | ||
| + | [[Category: Krell T]] | ||
| + | [[Category: Martinez-Rodriguez S]] | ||
Current revision
Ligand binding domain of the P. Putida receptor McpH in complex with Uric acid
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