380 related articles for article (PubMed ID: 15938615)
1. 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; 44(23):8260-6. PubMed ID: 15938615
[TBL] [Abstract][Full Text] [Related]
2. 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; 46(48):13920-8. PubMed ID: 17994765
[TBL] [Abstract][Full Text] [Related]
3. 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
[TBL] [Abstract][Full Text] [Related]
4. 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; 186(16):5519-22. PubMed ID: 15292155
[TBL] [Abstract][Full Text] [Related]
5. Functional modules of KdpB, the catalytic subunit of the Kdp-ATPase from Escherichia coli.
Bramkamp M; Altendorf K
Biochemistry; 2004 Sep; 43(38):12289-96. PubMed ID: 15379567
[TBL] [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; 47(11):3564-75. PubMed ID: 18298081
[TBL] [Abstract][Full Text] [Related]
7. FITC binding site and p-nitrophenyl phosphatase activity of the Kdp-ATPase of Escherichia coli.
Bramkamp M; Gassel M; Altendorf K
Biochemistry; 2004 Apr; 43(15):4559-67. PubMed ID: 15078102
[TBL] [Abstract][Full Text] [Related]
8. 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; 45(36):11038-46. PubMed ID: 16953591
[TBL] [Abstract][Full Text] [Related]
9. 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
[TBL] [Abstract][Full Text] [Related]
10. 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
[TBL] [Abstract][Full Text] [Related]
11. Glutamates 99 and 107 in transmembrane helix III of subunit I of cytochrome bd are critical for binding of the heme b595-d binuclear center and enzyme activity.
Mogi T; Endou S; Akimoto S; Morimoto-Tadokoro M; Miyoshi H
Biochemistry; 2006 Dec; 45(51):15785-92. PubMed ID: 17176101
[TBL] [Abstract][Full Text] [Related]
12. 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; 10(2-4):120-31. PubMed ID: 16645309
[TBL] [Abstract][Full Text] [Related]
13. Characterization of amino acid substitutions in KdpA, the K+-binding and -translocating subunit of the KdpFABC complex of Escherichia coli.
van der Laan M; Gassel M; Altendorf K
J Bacteriol; 2002 Oct; 184(19):5491-4. PubMed ID: 12218037
[TBL] [Abstract][Full Text] [Related]
14. Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex from Escherichia coli (Review).
Bramkamp M; Altendorf K; Greie JC
Mol Membr Biol; 2007; 24(5-6):375-86. PubMed ID: 17710642
[TBL] [Abstract][Full Text] [Related]
15. Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC.
Silberberg JM; Corey RA; Hielkema L; Stock C; Stansfeld PJ; Paulino C; Hänelt I
Nat Commun; 2021 Aug; 12(1):5098. PubMed ID: 34429416
[TBL] [Abstract][Full Text] [Related]
16. 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; 342(5):1547-58. PubMed ID: 15364580
[TBL] [Abstract][Full Text] [Related]
17. Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase.
Damnjanovic B; Weber A; Potschies M; Greie JC; Apell HJ
Biochemistry; 2013 Aug; 52(33):5563-76. PubMed ID: 23930894
[TBL] [Abstract][Full Text] [Related]
18. 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; 643():137-46. PubMed ID: 9789555
[TBL] [Abstract][Full Text] [Related]
19. Crystal structure of the potassium-importing KdpFABC membrane complex.
Huang CS; Pedersen BP; Stokes DL
Nature; 2017 Jun; 546(7660):681-685. PubMed ID: 28636601
[TBL] [Abstract][Full Text] [Related]
20. Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70.
Wilbanks SM; McKay DB
Biochemistry; 1998 May; 37(20):7456-62. PubMed ID: 9585559
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]