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8poo
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Low resolution structure of inactive conformation of the Ktr cation channel in presence of ATP and c-di-AMP== | |
| + | <StructureSection load='8poo' size='340' side='right'caption='[[8poo]], [[Resolution|resolution]] 5.77Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8poo]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8POO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8POO 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]] 5.77Å</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=8poo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8poo OCA], [https://pdbe.org/8poo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8poo RCSB], [https://www.ebi.ac.uk/pdbsum/8poo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8poo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KTRB_BACSU KTRB_BACSU] Integral membrane subunit of the KtrAB potassium uptake transporter. The 2 major potassium transporter complexes KtrAB and KtrCD confer resistance to both suddenly imposed and prolonged osmotic stress.<ref>PMID:12562800</ref> <ref>PMID:17932047</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In bacteria, intracellular K(+) is involved in the regulation of membrane potential, cytosolic pH, and cell turgor as well as in spore germination, environmental adaptation, cell-to-cell communication in biofilms, antibiotic sensitivity, and infectivity. The second messenger cyclic-di-AMP (c-di-AMP) has a central role in modulating the intracellular K(+) concentration in many bacterial species, controlling transcription and function of K(+) channels and transporters. However, our understanding of how this regulatory network responds to c-di-AMP remains poor. We used the RCK (Regulator of Conductance of K(+)) proteins that control the activity of Ktr channels in Bacillus subtilis as a model system to analyze the regulatory function of c-di-AMP with a combination of in vivo and in vitro functional and structural characterization. We determined that the two RCK proteins (KtrA and KtrC) are neither physiologically redundant or functionally equivalent. KtrC is the physiologically dominant RCK protein in the regulation of Ktr channel activity. In explaining this hierarchical organization, we found that, unlike KtrA, KtrC is very sensitive to c-di-AMP inactivation and lack of c-di-AMP regulation results in RCK protein toxicity, most likely due to unregulated K(+) flux. We also found that KtrC can assemble with KtrA, conferring c-di-AMP regulation to the functional KtrA/KtrC heteromers and potentially compensating KtrA toxicity. Altogether, we propose that the central role of c-di-AMP in the control of the K(+) machinery, by modulating protein levels through gene transcription and by regulating protein activity, has determined the evolutionary selection of KtrC as the dominant RCK protein, shaping the hierarchical organization of regulatory components of the K(+) machinery. | ||
| - | + | c-di-AMP determines the hierarchical organization of bacterial RCK proteins.,Rocha R, Jorge JMP, Teixeira-Duarte CM, Figueiredo-Costa IR, Cereija TB, Ferreira-Teixeira PF, Herzberg C, Stulke J, Morais-Cabral JH Proc Natl Acad Sci U S A. 2024 Apr 30;121(18):e2318666121. doi: , 10.1073/pnas.2318666121. Epub 2024 Apr 23. PMID:38652747<ref>PMID:38652747</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8poo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cereija TB]] | ||
| + | [[Category: Morais-Cabral JH]] | ||
| + | [[Category: Teixeira-Duarte CM]] | ||
Current revision
Low resolution structure of inactive conformation of the Ktr cation channel in presence of ATP and c-di-AMP
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