The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone

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dc.contributor.authorIrzik, Kristina
dc.contributor.authorPfroetzschner, Juliane
dc.contributor.authorGoss, Tatjana
dc.contributor.authorAhnert, Franziska
dc.contributor.authorHaupt, Melina
dc.contributor.authorGreie, Joerg-Christian
dc.date.accessioned2021-12-23T16:07:55Z-
dc.date.available2021-12-23T16:07:55Z-
dc.date.issued2011
dc.identifier.issn1742464X
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/8137-
dc.description.abstractIn Bacteria and Archaea, high-affinity potassium uptake is mediated by the ATP-driven KdpFABC complex. On the basis of the biochemical properties of the ATP-hydrolyzing subunit KdpB, the transport complex is classified as type IA P-type ATPase. However, the KdpA subunit, which promotes K+ transport, clearly resembles a potassium channel, such that the KdpFABC complex represents a chimera of ion pumps and ion channels. In the present study, we demonstrate that the blending of these two groups of transporters in KdpFABC also entails a nucleotide-binding mechanism in which the KdpC subunit acts as a catalytic chaperone. This mechanism is found neither in P-type ATPases nor in ion channels, although parallels are found in ABC transporters. In the latter, the ATP nucleotide is coordinated by the LSGGQ signature motif via double hydrogen bonds at a conserved glutamine residue, which is also present in KdpC. High-affinity nucleotide binding to the KdpFABC complex was dependent on the presence of this conserved glutamine residue in KdpC. In addition, both ATP binding to KdpC and ATP hydrolysis activity of KdpFABC were sensitive to the accessibility, presence or absence of the hydroxyl groups at the ribose moiety of the nucleotide. Furthermore, the KdpC subunit was shown to interact with the nucleotide-binding loop of KdpB in an ATP-dependent manner around the ATP-binding pocket, thereby increasing the ATP-binding affinity by the formation of a transient KdpB/KdpC/ATP ternary complex.
dc.description.sponsorshipDeutsche Forschungsgemeinschaft, DFGGerman Research Foundation (DFG) [SFB 431/P7]; Brigitte Herkenhoff-Hesselmann is kindly acknowledged for the preparation of <SUP>15</SUP>N-labeled KdpBN. Johann Klare is kindly acknowledged for assisting with the ITC analyses and Henrik Strahl is thanked for help with the molecular modeling and sequence alignment. This work was supported by the Deutsche Forschungsgemeinschaft, DFG (SFB 431/P7).
dc.language.isoen
dc.publisherWILEY
dc.relation.ispartofFEBS JOURNAL
dc.subjectABC transporter
dc.subjectBiochemistry & Molecular Biology
dc.subjectCA2+-ATPASE
dc.subjection pump
dc.subjectKdpFABC
dc.subjectKDPFABC COMPLEX
dc.subjectN-DOMAIN
dc.subjectNUCLEOTIDE-BINDING DOMAIN
dc.subjectP-type ATPase
dc.subjectpotassium transport
dc.subjectPROTEIN
dc.titleThe KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone
dc.typejournal article
dc.identifier.doi10.1111/j.1742-4658.2011.08224.x
dc.identifier.isiISI:000294025800008
dc.description.volume278
dc.description.issue17
dc.description.startpage3041
dc.description.endpage3053
dc.identifier.eissn17424658
dc.publisher.place111 RIVER ST, HOBOKEN 07030-5774, NJ USA
dcterms.isPartOf.abbreviationFEBS J.
dcterms.oaStatusBronze
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