4J7C
KtrAB potassium transporter from Bacillus subtilis
Summary for 4J7C
| Entry DOI | 10.2210/pdb4j7c/pdb |
| Related | 4J90 4J91 |
| Descriptor | Ktr system potassium uptake protein A, Ktr system potassium uptake protein B, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | ktrb pore-forming membrane protein, ktra regulatory cytosolic ring, potassium ion transport, potassium, cell membrane, cytosol, transport protein |
| Biological source | Bacillus subtilis More |
| Cellular location | Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): O32080 Cell membrane; Multi-pass membrane protein (Potential): O32081 |
| Total number of polymer chains | 12 |
| Total formula weight | 406087.39 |
| Authors | Vieira-Pires, R.S.,Morais-Cabral, J.H. (deposition date: 2013-02-13, release date: 2013-04-17, Last modification date: 2023-11-08) |
| Primary citation | Vieira-Pires, R.S.,Szollosi, A.,Morais-Cabral, J.H. The structure of the KtrAB potassium transporter Nature, 496:323-328, 2013 Cited by PubMed Abstract: 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. PubMed: 23598340DOI: 10.1038/nature12055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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