The KdpFABC complex from Escherichia coli: A chimeric K + transporter merging ion pumps with ion channels

• Published in: European journal of cell biology Vol. 90; no. 9; pp. 705 - 710
• Main Author: Greie, Jörg-Christian
• Format: Journal Article
• Language: English
• Published: Germany Elsevier GmbH 01.09.2011
• Subjects: ABC transporter; Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; Cation Transport Proteins - chemistry; Cation Transport Proteins - metabolism; Escherichia coli - chemistry; Escherichia coli - enzymology; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Ion channel; Ion Transport; KdpFABC; Models, Molecular; P-type ATPase; Potassium transport; Protein Structure, Secondary; KdpFABC; Potassium transport; Ion channel; ABC transporter; P-type ATPase
• ISSN: 0171-9335; 1618-1298
• DOI: 10.1016/j.ejcb.2011.04.011

The KdpFABC complex represents a multi-subunit ATP-driven potassium pump, which is only found in bacteria and archaea. Based on the properties of the ATP-hydrolyzing subunit (KdpB) the transporter has been classified as a type IA P-type ATPase. However, structural and functional properties of the remaining subunits clearly show homologies to members of the potassium channel as well as the ABC transporter family, thus rendering the KdpFABC complex to represent an inimitable chimera of ion pumps and ion channels. Accordingly, this striking juxtaposition entails special features of KdpFABC with respect to typical members of each of the transporter families, involving not only the concepts but also the structures of ion channels and ion pumps. For example, the sites of ATP hydrolysis and substrate transport are spatially separated on two different polypeptides, which, in turn, leads to a unique coupling mechanism. During catalysis, the KdpFABC complex cycles between two main conformational states, each of which comprises different structural properties together with different binding affinities for both ATP and the transport substrate. These structural configurations have recently been directly visualized in the working enzyme. Translocation of potassium is mediated by the KdpA subunit, which comprises structural as well as functional homologies to potassium channels of the MPM-type. The KdpC subunit participates in the binding of ATP, thus acting as a catalytic chaperone, which increases the ATP binding affinity of the KdpB subunit via a mechanism typical of nucleotide binding in ABC transporters.