Does the KdpA subunit from the high affinity K+-translocating P-type KDP-ATPase have a structure similar to that of K+ channels?

DC FieldValueLanguage
dc.contributor.authorDurell, SR
dc.contributor.authorBakker, EP
dc.contributor.authorGuy, HR
dc.date.accessioned2021-12-23T16:13:32Z-
dc.date.available2021-12-23T16:13:32Z-
dc.date.issued2000
dc.identifier.issn00063495
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/10617-
dc.description.abstractEvidence is presented that the transmembrane KdpA subunit of the high affinity K+-translocating P-type Kdp-ATPase is evolutionarily derived from the superfamily of 2TM-type K+ channels in bacteria. This extends a previous study relating the K+ channels to the KtrAB, Trk, Trk1,2, and HKT1 K+ symporter superfamily of both prokaryotes and eukaryotes, Although the channels are formed by four single-MPM motif subunits, the transmembrane KdpA subunit and the transmembrane subunit of the symporter proteins are postulated to have four corresponding MPM motifs within a single sequence. Analysis of 17 KdpA sequences reveals a pattern of residue conservation similar to that of the symporters and channels, and consistent with the crystal structure of the KcsA K+ channel. In addition, the most highly conserved residues between the families, specifically the central glycines of the P2 segments, are those previously identified as crucial for the property of K+-selectivity that is common to each protein. This hypothesis is consistent with an experimental study of mutations that alter K+ binding affinity of the Kdp transporter. Although most of the results of a previous study of the transmembrane topology of KdpA are consistent with the 4-MPM model, the one deviation can be explained by a plausible change in the structure due to the experimental method.
dc.description.sponsorshipDIVISION OF BASIC SCIENCES - NCIUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Cancer Institute (NCI) [Z01BC008363] Funding Source: NIH RePORTER
dc.language.isoen
dc.publisherCELL PRESS
dc.relation.ispartofBIOPHYSICAL JOURNAL
dc.subjectBiophysics
dc.subjectHKT1
dc.subjectPOTASSIUM CHANNEL
dc.subjectTRANSPORT ATPASES
dc.titleDoes the KdpA subunit from the high affinity K+-translocating P-type KDP-ATPase have a structure similar to that of K+ channels?
dc.typejournal article
dc.identifier.doi10.1016/S0006-3495(00)76584-2
dc.identifier.isiISI:000084772900018
dc.description.volume78
dc.description.issue1, 1
dc.description.startpage188
dc.description.endpage199
dc.identifier.eissn15420086
dc.publisher.place50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA
dcterms.isPartOf.abbreviationBiophys. J.
dcterms.oaStatusBronze, Green Published
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