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364 related items for PubMed ID: 14510639

  • 1. The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP.
    Okkeri J, Laakkonen L, Haltia T.
    Biochem J; 2004 Jan 01; 377(Pt 1):95-105. PubMed ID: 14510639
    [Abstract] [Full Text] [Related]

  • 2. Metal-binding characteristics of the amino-terminal domain of ZntA: binding of lead is different compared to cadmium and zinc.
    Liu J, Stemmler AJ, Fatima J, Mitra B.
    Biochemistry; 2005 Apr 05; 44(13):5159-67. PubMed ID: 15794653
    [Abstract] [Full Text] [Related]

  • 3. The structure of Mg-ATPase nucleotide-binding domain at 1.6 A resolution reveals a unique ATP-binding motif.
    Håkansson KO.
    Acta Crystallogr D Biol Crystallogr; 2009 Nov 05; 65(Pt 11):1181-6. PubMed ID: 19923713
    [Abstract] [Full Text] [Related]

  • 4. 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
    [Abstract] [Full Text] [Related]

  • 5. Expression and mutagenesis of ZntA, a zinc-transporting P-type ATPase from Escherichia coli.
    Okkeri J, Haltia T.
    Biochemistry; 1999 Oct 19; 38(42):14109-16. PubMed ID: 10529259
    [Abstract] [Full Text] [Related]

  • 6. Role of the insertion domain and the zinc-finger motif of Escherichia coli UvrA in damage recognition and ATP hydrolysis.
    Wagner K, Moolenaar GF, Goosen N.
    DNA Repair (Amst); 2011 May 05; 10(5):483-96. PubMed ID: 21393072
    [Abstract] [Full Text] [Related]

  • 7. Conservative and nonconservative mutations of the transmembrane CPC motif in ZntA: effect on metal selectivity and activity.
    Dutta SJ, Liu J, Stemmler AJ, Mitra B.
    Biochemistry; 2007 Mar 27; 46(12):3692-703. PubMed ID: 17326661
    [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 12; 45(36):11038-46. PubMed ID: 16953591
    [Abstract] [Full Text] [Related]

  • 9. Conserved aspartic acid 714 in transmembrane segment 8 of the ZntA subgroup of P1B-type ATPases is a metal-binding residue.
    Dutta SJ, Liu J, Hou Z, Mitra B.
    Biochemistry; 2006 May 09; 45(18):5923-31. PubMed ID: 16669635
    [Abstract] [Full Text] [Related]

  • 10. Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity.
    Li J, Sha B.
    J Mol Biol; 2002 May 10; 318(4):1127-37. PubMed ID: 12054807
    [Abstract] [Full Text] [Related]

  • 11. The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase.
    Bordelon T, Nilsson Lill SO, Waldrop GL.
    Proteins; 2009 Mar 10; 74(4):808-19. PubMed ID: 18704941
    [Abstract] [Full Text] [Related]

  • 12. Novel Zn2+ coordination by the regulatory N-terminus metal binding domain of Arabidopsis thaliana Zn(2+)-ATPase HMA2.
    Eren E, González-Guerrero M, Kaufman BM, Argüello JM.
    Biochemistry; 2007 Jul 03; 46(26):7754-64. PubMed ID: 17550234
    [Abstract] [Full Text] [Related]

  • 13. Study of the ATP-binding site of helicase IV from Escherichia coli.
    Dubaele S, Lourdel C, Chène P.
    Biochem Biophys Res Commun; 2006 Mar 17; 341(3):828-36. PubMed ID: 16442499
    [Abstract] [Full Text] [Related]

  • 14. Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase.
    Fodje MN, Hansson A, Hansson M, Olsen JG, Gough S, Willows RD, Al-Karadaghi S.
    J Mol Biol; 2001 Aug 03; 311(1):111-22. PubMed ID: 11469861
    [Abstract] [Full Text] [Related]

  • 15. Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes.
    Hall MC, Ozsoy AZ, Matson SW.
    J Mol Biol; 1998 Mar 27; 277(2):257-71. PubMed ID: 9514760
    [Abstract] [Full Text] [Related]

  • 16. Structure of dimeric SecA, the Escherichia coli preprotein translocase motor.
    Papanikolau Y, Papadovasilaki M, Ravelli RB, McCarthy AA, Cusack S, Economou A, Petratos K.
    J Mol Biol; 2007 Mar 09; 366(5):1545-57. PubMed ID: 17229438
    [Abstract] [Full Text] [Related]

  • 17. The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase.
    Lánský Z, Kubala M, Ettrich R, Kutý M, Plásek J, Teisinger J, Schoner W, Amler E.
    Biochemistry; 2004 Jul 06; 43(26):8303-11. PubMed ID: 15222743
    [Abstract] [Full Text] [Related]

  • 18. Introducing Wilson disease mutations into the zinc-transporting P-type ATPase of Escherichia coli. The mutation P634L in the 'hinge' motif (GDGXNDXP) perturbs the formation of the E2P state.
    Okkeri J, Bencomo E, Pietilä M, Haltia T.
    Eur J Biochem; 2002 Mar 06; 269(5):1579-86. PubMed ID: 11874474
    [Abstract] [Full Text] [Related]

  • 19. 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
    [Abstract] [Full Text] [Related]

  • 20. The structure and function of heavy metal transport P1B-ATPases.
    Argüello JM, Eren E, González-Guerrero M.
    Biometals; 2007 Jun 28; 20(3-4):233-48. PubMed ID: 17219055
    [Abstract] [Full Text] [Related]

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