9EMB
Structure of KefC Asp156Asn variant
Summary for 9EMB
| Entry DOI | 10.2210/pdb9emb/pdb |
| Related | 8BXG 8BY2 |
| EMDB information | 19816 |
| Descriptor | Glutathione-regulated potassium-efflux system protein KefC, ADENOSINE MONOPHOSPHATE, (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate (3 entities in total) |
| Functional Keywords | kefc, potassium, gsh, mutant, transport protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 124556.93 |
| Authors | Gulati, A.,Kokane, S.,Drew, D. (deposition date: 2024-03-07, release date: 2024-06-05, Last modification date: 2025-01-29) |
| Primary citation | Gulati, A.,Kokane, S.,Perez-Boerema, A.,Alleva, C.,Meier, P.F.,Matsuoka, R.,Drew, D. Structure and mechanism of the K + /H + exchanger KefC. Nat Commun, 15:4751-4751, 2024 Cited by PubMed Abstract: Intracellular potassium (K) homeostasis is fundamental to cell viability. In addition to channels, K levels are maintained by various ion transporters. One major family is the proton-driven K efflux transporters, which in gram-negative bacteria is important for detoxification and in plants is critical for efficient photosynthesis and growth. Despite their importance, the structure and molecular basis for K-selectivity is poorly understood. Here, we report ~3.1 Å resolution cryo-EM structures of the Escherichia coli glutathione (GSH)-gated K efflux transporter KefC in complex with AMP, AMP/GSH and an ion-binding variant. KefC forms a homodimer similar to the inward-facing conformation of Na/H antiporter NapA. By structural assignment of a coordinated K ion, MD simulations, and SSM-based electrophysiology, we demonstrate how ion-binding in KefC is adapted for binding a dehydrated K ion. KefC harbors C-terminal regulator of K conductance (RCK) domains, as present in some bacterial K-ion channels. The domain-swapped helices in the RCK domains bind AMP and GSH and they inhibit transport by directly interacting with the ion-transporter module. Taken together, we propose that KefC is activated by detachment of the RCK domains and that ion selectivity exploits the biophysical properties likewise adapted by K-ion-channels. PubMed: 38834573DOI: 10.1038/s41467-024-49082-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.98 Å) |
Structure validation
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