|
|
| Line 3: |
Line 3: |
| | <StructureSection load='7ahm' size='340' side='right'caption='[[7ahm]], [[Resolution|resolution]] 3.14Å' scene=''> | | <StructureSection load='7ahm' size='340' side='right'caption='[[7ahm]], [[Resolution|resolution]] 3.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7ahm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AHM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ahm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AHM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BA:(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,10,12-TETROL+5,12-DIOXIDE'>2BA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.14Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7agv|7agv]], [[7agy|7agy]], [[7agw|7agw]], [[7aht|7aht]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BA:(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,10,12-TETROL+5,12-DIOXIDE'>2BA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">khtT, yhaT, BSU09860 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</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=7ahm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ahm OCA], [https://pdbe.org/7ahm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ahm RCSB], [https://www.ebi.ac.uk/pdbsum/7ahm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ahm ProSAT]</span></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=7ahm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ahm OCA], [https://pdbe.org/7ahm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ahm RCSB], [https://www.ebi.ac.uk/pdbsum/7ahm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ahm ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/KHTT_BACSU KHTT_BACSU]] Required for activity of the potassium/proton antiporter KhtU (PubMed:14987767, PubMed:17679694). Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis (PubMed:24330391).<ref>PMID:14987767</ref> <ref>PMID:17679694</ref> <ref>PMID:24330391</ref>
| + | [https://www.uniprot.org/uniprot/KHTT_BACSU KHTT_BACSU] Required for activity of the potassium/proton antiporter KhtU (PubMed:14987767, PubMed:17679694). Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis (PubMed:24330391).<ref>PMID:14987767</ref> <ref>PMID:17679694</ref> <ref>PMID:24330391</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cereija, T B]] | + | [[Category: Cereija TB]] |
| - | [[Category: Guerra, J P]] | + | [[Category: Guerra JP]] |
| - | [[Category: Morais-Cabral, J H]] | + | [[Category: Morais-Cabral JH]] |
| - | [[Category: C-di-amp binding protein]]
| + | |
| - | [[Category: Regulatory protein of k+/h+ antiporter]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
KHTT_BACSU Required for activity of the potassium/proton antiporter KhtU (PubMed:14987767, PubMed:17679694). Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis (PubMed:24330391).[1] [2] [3]
Publication Abstract from PubMed
bis-(3',5')-cyclic diadenosine monophosphate (c-di-AMP) is a second messenger with roles in virulence, cell wall and biofilm formation, and surveillance of DNA integrity in many bacterial species, including pathogens. Strikingly, it has also been proposed to coordinate the activity of the components of K(+) homeostasis machinery, inhibiting K(+) import, and activating K(+) export. However, there is a lack of quantitative evidence supporting the direct functional impact of c-di-AMP on K(+) transporters. To gain a detailed understanding of the role of c-di-AMP on the activity of a component of the K(+) homeostasis machinery in B. subtilis, we have characterized the impact of c-di-AMP on the functional, biochemical, and physiological properties of KhtTU, a K(+)/H(+) antiporter composed of the membrane protein KhtU and the cytosolic protein KhtT. We have confirmed c-di-AMP binding to KhtT and determined the crystal structure of this complex. We have characterized in vitro the functional properties of KhtTU and KhtU alone and quantified the impact of c-di-AMP and of pH on their activity, demonstrating that c-di-AMP activates KhtTU and that pH increases its sensitivity to this nucleotide. Based on our functional and structural data, we were able to propose a mechanism for the activation of KhtTU by c-di-AMP. In addition, we have analyzed the impact of KhtTU in its native bacterium, providing a physiological context for the regulatory function of c-di-AMP and pH. Overall, we provide unique information that supports the proposal that c-di-AMP is a master regulator of K+ homeostasis machinery.
c-di-AMP, a likely master regulator of bacterial K(+) homeostasis machinery, activates a K(+) exporter.,Cereija TB, Guerra JPL, Jorge JMP, Morais-Cabral JH Proc Natl Acad Sci U S A. 2021 Apr 6;118(14). pii: 2020653118. doi:, 10.1073/pnas.2020653118. PMID:33790011[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujisawa M, Wada Y, Ito M. Modulation of the K+ efflux activity of Bacillus subtilis YhaU by YhaT and the C-terminal region of YhaS. FEMS Microbiol Lett. 2004 Feb 16;231(2):211-7. doi:, 10.1016/S0378-1097(03)00959-5. PMID:14987767 doi:http://dx.doi.org/10.1016/S0378-1097(03)00959-5
- ↑ Fujisawa M, Ito M, Krulwich TA. Three two-component transporters with channel-like properties have monovalent cation/proton antiport activity. Proc Natl Acad Sci U S A. 2007 Aug 14;104(33):13289-94. doi:, 10.1073/pnas.0703709104. Epub 2007 Aug 6. PMID:17679694 doi:http://dx.doi.org/10.1073/pnas.0703709104
- ↑ Chandrangsu P, Dusi R, Hamilton CJ, Helmann JD. Methylglyoxal resistance in Bacillus subtilis: contributions of bacillithiol-dependent and independent pathways. Mol Microbiol. 2014 Feb;91(4):706-15. doi: 10.1111/mmi.12489. Epub 2014 Jan 7. PMID:24330391 doi:http://dx.doi.org/10.1111/mmi.12489
- ↑ Cereija TB, Guerra JPL, Jorge JMP, Morais-Cabral JH. c-di-AMP, a likely master regulator of bacterial K(+) homeostasis machinery, activates a K(+) exporter. Proc Natl Acad Sci U S A. 2021 Apr 6;118(14). pii: 2020653118. doi:, 10.1073/pnas.2020653118. PMID:33790011 doi:http://dx.doi.org/10.1073/pnas.2020653118
|
