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144 related items for PubMed ID: 19285138

  • 1. Solution structure of the KdpFABC P-type ATPase from Escherichia coli by electron microscopic single particle analysis.
    Heitkamp T, Böttcher B, Greie JC.
    J Struct Biol; 2009 Jun; 166(3):295-302. PubMed ID: 19285138
    [Abstract] [Full Text] [Related]

  • 2. The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone.
    Irzik K, Pfrötzschner J, Goss T, Ahnert F, Haupt M, Greie JC.
    FEBS J; 2011 Sep; 278(17):3041-53. PubMed ID: 21711450
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  • 3. The KdpFABC complex from Escherichia coli: a chimeric K+ transporter merging ion pumps with ion channels.
    Greie JC.
    Eur J Cell Biol; 2011 Sep; 90(9):705-10. PubMed ID: 21684627
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  • 4. Single amino acid substitution in the putative transmembrane helix V in KdpB of the KdpFABC complex of Escherichia coli uncouples ATPase activity and ion transport.
    Bramkamp M, Altendorf K.
    Biochemistry; 2005 Jun 14; 44(23):8260-6. PubMed ID: 15938615
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  • 5. ATP binding properties of the soluble part of the KdpC subunit from the Escherichia coli K(+)-transporting KdpFABC P-type ATPase.
    Ahnert F, Schmid R, Altendorf K, Greie JC.
    Biochemistry; 2006 Sep 12; 45(36):11038-46. PubMed ID: 16953591
    [Abstract] [Full Text] [Related]

  • 6. K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer.
    Heitkamp T, Kalinowski R, Böttcher B, Börsch M, Altendorf K, Greie JC.
    Biochemistry; 2008 Mar 18; 47(11):3564-75. PubMed ID: 18298081
    [Abstract] [Full Text] [Related]

  • 7. The conserved dipole in transmembrane helix 5 of KdpB in the Escherichia coli KdpFABC P-type ATPase is crucial for coupling and the electrogenic K+-translocation step.
    Becker D, Fendler K, Altendorf K, Greie JC.
    Biochemistry; 2007 Dec 04; 46(48):13920-8. PubMed ID: 17994765
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  • 9. Inter-domain motions of the N-domain of the KdpFABC complex, a P-type ATPase, are not driven by ATP-induced conformational changes.
    Haupt M, Bramkamp M, Coles M, Altendorf K, Kessler H.
    J Mol Biol; 2004 Oct 01; 342(5):1547-58. PubMed ID: 15364580
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  • 10. Functional modules of KdpB, the catalytic subunit of the Kdp-ATPase from Escherichia coli.
    Bramkamp M, Altendorf K.
    Biochemistry; 2004 Sep 28; 43(38):12289-96. PubMed ID: 15379567
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  • 14. Structure and function of the Kdp-ATPase of Escherichia coli.
    Altendorf K, Gassel M, Puppe W, Möllenkamp T, Zeeck A, Boddien C, Fendler K, Bamberg E, Dröse S.
    Acta Physiol Scand Suppl; 1998 Aug 28; 643():137-46. PubMed ID: 9789555
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  • 15. Prokaryotic Kdp-ATPase: recent insights into the structure and function of KdpB.
    Haupt M, Bramkamp M, Coles M, Kessler H, Altendorf K.
    J Mol Microbiol Biotechnol; 2005 Aug 28; 10(2-4):120-31. PubMed ID: 16645309
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  • 16. Structural basis for potassium transport in prokaryotes by KdpFABC.
    Sweet ME, Larsen C, Zhang X, Schlame M, Pedersen BP, Stokes DL.
    Proc Natl Acad Sci U S A; 2021 Jul 20; 118(29):. PubMed ID: 34272288
    [Abstract] [Full Text] [Related]

  • 17. Amino acid substitutions in putative selectivity filter regions III and IV in KdpA alter ion selectivity of the KdpFABC complex from Escherichia coli.
    Bertrand J, Altendorf K, Bramkamp M.
    J Bacteriol; 2004 Aug 20; 186(16):5519-22. PubMed ID: 15292155
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  • 18. Role of protons in the pump cycle of KdpFABC investigated by time-resolved kinetic experiments.
    Damnjanovic B, Apell HJ.
    Biochemistry; 2014 May 20; 53(19):3218-28. PubMed ID: 24766073
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  • 20. Crystal structure of the potassium-importing KdpFABC membrane complex.
    Huang CS, Pedersen BP, Stokes DL.
    Nature; 2017 Jun 29; 546(7660):681-685. PubMed ID: 28636601
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