7NNL
Cryo-EM structure of the KdpFABC complex in an E1-ATP conformation loaded with K+
Summary for 7NNL
| Entry DOI | 10.2210/pdb7nnl/pdb |
| Related | 7NNP |
| EMDB information | 12478 12482 |
| Descriptor | Potassium-transporting ATPase potassium-binding subunit, Potassium-transporting ATPase KdpC subunit, Potassium-transporting ATPase KdpF subunit, ... (7 entities in total) |
| Functional Keywords | p-type atpase, superfamily of k+ transporters (skt), potassium uptake system, atp analogue, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 158524.24 |
| Authors | Silberberg, J.M.,Corey, R.A.,Hielkema, L.,Stock, C.,Stansfeld, P.J.,Paulino, C.,Haenelt, I. (deposition date: 2021-02-25, release date: 2021-07-28, Last modification date: 2024-10-23) |
| Primary citation | Silberberg, J.M.,Corey, R.A.,Hielkema, L.,Stock, C.,Stansfeld, P.J.,Paulino, C.,Hanelt, I. Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC. Nat Commun, 12:5098-5098, 2021 Cited by PubMed Abstract: KdpFABC, a high-affinity K pump, combines the ion channel KdpA and the P-type ATPase KdpB to secure survival at K limitation. Here, we apply a combination of cryo-EM, biochemical assays, and MD simulations to illuminate the mechanisms underlying transport and the coupling to ATP hydrolysis. We show that ions are transported via an intersubunit tunnel through KdpA and KdpB. At the subunit interface, the tunnel is constricted by a phenylalanine, which, by polarized cation-π stacking, controls K entry into the canonical substrate binding site (CBS) of KdpB. Within the CBS, ATPase coupling is mediated by the charge distribution between an aspartate and a lysine. Interestingly, individual elements of the ion translocation mechanism of KdpFABC identified here are conserved among a wide variety of P-type ATPases from different families. This leads us to the hypothesis that KdpB might represent an early descendant of a common ancestor of cation pumps. PubMed: 34429416DOI: 10.1038/s41467-021-25242-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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