5BUT
Crystal structure of inactive conformation of KtrAB K+ transporter
Summary for 5BUT
| Entry DOI | 10.2210/pdb5but/pdb |
| Descriptor | Ktr system potassium uptake protein A,Ktr system potassium uptake protein A, Ktr system potassium uptake protein B, POTASSIUM ION (3 entities in total) |
| Functional Keywords | membrane protein complex, membrane protein |
| Biological source | Bacillus subtilis More |
| Cellular location | Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : O32080 Cell membrane ; Multi-pass membrane protein : O32081 |
| Total number of polymer chains | 8 |
| Total formula weight | 320943.42 |
| Authors | Vieira-Pires, R.S.,Morais-Cabral, J.H. (deposition date: 2015-06-04, release date: 2016-01-27, Last modification date: 2024-01-10) |
| Primary citation | Szollosi, A.,Vieira-Pires, R.S.,Teixeira-Duarte, C.M.,Rocha, R.,Morais-Cabral, J.H. Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter. Plos Biol., 14:e1002356-e1002356, 2016 Cited by PubMed Abstract: KtrAB belongs to the Trk/Ktr/HKT superfamily of monovalent cation (K+ and Na+) transport proteins that closely resemble K+ channels. These proteins underlie a plethora of cellular functions that are crucial for environmental adaptation in plants, fungi, archaea, and bacteria. The activation mechanism of the Trk/Ktr/HKT proteins remains unknown. It has been shown that ATP stimulates the activity of KtrAB while ADP does not. Here, we present X-ray structural information on the KtrAB complex with bound ADP. A comparison with the KtrAB-ATP structure reveals conformational changes in the ring and in the membrane protein. In combination with a biochemical and functional analysis, we uncover how ligand-dependent changes in the KtrA ring are propagated to the KtrB membrane protein and conclude that, despite their structural similarity, the activation mechanism of KtrAB is markedly different from the activation mechanism of K+ channels. PubMed: 26771197DOI: 10.1371/journal.pbio.1002356 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (5.97 Å) |
Structure validation
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