Cryo-EM structure of the KdpFABC complex in an E1-ATP conformation loaded with K+

PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE

DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL

Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC.

10 mM Tris-HCl pH 8, 10 mM MgCl2, 10 mM NaCl and 0.0125% DDM

Potassium-transporting ATPase potassium-binding subunit

Potassium-transporting ATPase KdpC subunit

Potassium-transporting ATPase KdpF subunit

Potassium-transporting ATPase ATP-binding subunit

ATP phosphohydrolase [potassium-transporting] A chain,Potassium-binding and translocating subunit A,Potassium-translocating ATPase A chain

ATP phosphohydrolase [potassium-transporting] C chain,Potassium-binding and translocating subunit C,Potassium-translocating ATPase C chain

ATP phosphohydrolase [potassium-transporting] F chain,Potassium-binding and translocating subunit F,Potassium-translocating ATPase F chain

ATP phosphohydrolase [potassium-transporting] B chain,Potassium-binding and translocating subunit B,Potassium-translocating ATPase B chain

Netherlands Organisation for Scientific Research (NWO)

P-type ATPase, superfamily of K+ transporters (SKT), potassium uptake system, ATP analogue, MEMBRANE PROTEIN