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| | ==KtrAB potassium transporter from Bacillus subtilis== | | ==KtrAB potassium transporter from Bacillus subtilis== |
| - | <StructureSection load='4j7c' size='340' side='right' caption='[[4j7c]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='4j7c' size='340' side='right'caption='[[4j7c]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j7c]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J7C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j7c]] is a 12 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=4J7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J7C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j90|4j90]], [[4j91|4j91]]</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=4j7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j7c OCA], [https://pdbe.org/4j7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j7c RCSB], [https://www.ebi.ac.uk/pdbsum/4j7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j7c ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ktrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU]), ktrB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j7c OCA], [http://pdbe.org/4j7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j7c RCSB], [http://www.ebi.ac.uk/pdbsum/4j7c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j7c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KTRA_BACSU KTRA_BACSU]] Catalytic 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> [[http://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> | + | [https://www.uniprot.org/uniprot/KTRA_BACSU KTRA_BACSU] Catalytic 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Morais-Cabral, J H]] | + | [[Category: Large Structures]] |
| - | [[Category: Vieira-Pires, R S]] | + | [[Category: Morais-Cabral JH]] |
| - | [[Category: Cell membrane]] | + | [[Category: Vieira-Pires RS]] |
| - | [[Category: Cytosol]]
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| - | [[Category: Ktra regulatory cytosolic ring]]
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| - | [[Category: Ktrb pore-forming membrane protein]]
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| - | [[Category: Potassium]]
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| - | [[Category: Potassium ion transport]]
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| - | [[Category: Transport protein]]
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| Structural highlights
Function
KTRA_BACSU Catalytic 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.[1]
Publication Abstract from PubMed
In bacteria, archaea, fungi and plants the Trk, Ktr and HKT ion transporters are key components of osmotic regulation, pH homeostasis and resistance to drought and high salinity. These ion transporters are functionally diverse: they can function as Na(+) or K(+) channels and possibly as cation/K(+) symporters. They are closely related to potassium channels both at the level of the membrane protein and at the level of the cytosolic regulatory domains. Here we describe the crystal structure of a Ktr K(+) transporter, the KtrAB complex from Bacillus subtilis. The structure shows the dimeric membrane protein KtrB assembled with a cytosolic octameric KtrA ring bound to ATP, an activating ligand. A comparison between the structure of KtrAB-ATP and the structures of the isolated full-length KtrA protein with ATP or ADP reveals a ligand-dependent conformational change in the octameric ring, raising new ideas about the mechanism of activation in these transporters.
The structure of the KtrAB potassium transporter.,Vieira-Pires RS, Szollosi A, Morais-Cabral JH Nature. 2013 Apr 18;496(7445):323-8. doi: 10.1038/nature12055. PMID:23598340[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Holtmann G, Bakker EP, Uozumi N, Bremer E. KtrAB and KtrCD: two K+ uptake systems in Bacillus subtilis and their role in adaptation to hypertonicity. J Bacteriol. 2003 Feb;185(4):1289-98. PMID:12562800
- ↑ Vieira-Pires RS, Szollosi A, Morais-Cabral JH. The structure of the KtrAB potassium transporter. Nature. 2013 Apr 18;496(7445):323-8. doi: 10.1038/nature12055. PMID:23598340 doi:10.1038/nature12055
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