6CTF
Crystal structure of GltPh fast mutant - R276S/M395R
Summary for 6CTF
| Entry DOI | 10.2210/pdb6ctf/pdb |
| Descriptor | Glutamate transporter homolog, ASPARTIC ACID, SODIUM ION (3 entities in total) |
| Functional Keywords | transporter, ligand-bound, membrane protein |
| Biological source | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
| Total number of polymer chains | 3 |
| Total formula weight | 130513.06 |
| Authors | Boudker, O.,Oh, S. (deposition date: 2018-03-23, release date: 2018-10-10, Last modification date: 2024-10-23) |
| Primary citation | Oh, S.,Boudker, O. Kinetic mechanism of coupled binding in sodium-aspartate symporter GltPh. Elife, 7:-, 2018 Cited by PubMed Abstract: Many secondary active membrane transporters pump substrates against concentration gradients by coupling their uptake to symport of sodium ions. Symport requires the substrate and ions to be always transported together. Cooperative binding of the solutes is a key mechanism contributing to coupled transport in the sodium and aspartate symporter from Glt. Here, we describe the kinetic mechanism of coupled binding for Glt in the inward facing state. The first of the three coupled sodium ions, binds weakly and slowly, enabling the protein to accept the rest of the ions and the substrate. The last ion binds tightly, but is in rapid equilibrium with solution. Its release is required for the complex disassembly. Thus, the first ion serves to 'open the door' for the substrate, the last ion 'locks the door' once the substrate is in, and one ion contributes to both events. PubMed: 30255846DOI: 10.7554/eLife.37291 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.05 Å) |
Structure validation
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