1LSS
KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+
Summary for 1LSS
| Entry DOI | 10.2210/pdb1lss/pdb |
| Related | 1LSU |
| Descriptor | Trk system potassium uptake protein trkA homolog, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | ktn domain, nad, rck domain, potassium transport, potassium channel, ktra, rossmann fold, transport protein |
| Biological source | Methanocaldococcus jannaschii |
| Total number of polymer chains | 4 |
| Total formula weight | 63524.10 |
| Authors | Roosild, T.P.,Miller, S.,Booth, I.R.,Choe, S. (deposition date: 2002-05-18, release date: 2002-07-03, Last modification date: 2024-02-14) |
| Primary citation | Roosild, T.P.,Miller, S.,Booth, I.R.,Choe, S. A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch. Cell(Cambridge,Mass.), 109:781-791, 2002 Cited by PubMed Abstract: The regulation of cation content is critical for cell growth. However, the molecular mechanisms that gate the systems that control K+ movements remain unclear. KTN is a highly conserved cytoplasmic domain present ubiquitously in a variety of prokaryotic and eukaryotic K+ channels and transporters. Here we report crystal structures for two representative KTN domains that reveal a dimeric hinged assembly. Alternative ligands NAD+ and NADH block or vacate, respectively, the hinge region affecting the dimer's conformational flexibility. Conserved, surface-exposed hydrophobic patches that become coplanar upon hinge closure provide an assembly interface for KTN tetramerization. Mutational analysis using the KefC system demonstrates that this domain directly interacts with its respective transmembrane constituent, coupling ligand-mediated KTN conformational changes to the permease's activity. PubMed: 12086676DOI: 10.1016/S0092-8674(02)00768-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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