메뉴 건너뛰기




Volumn 348, Issue 1, 2006, Pages 124-131

Role of metal-binding domains of the copper pump from Archaeoglobus fulgidus

Author keywords

CopA; Copper pump; Extremophile; Membrane protein; Metal binding domain; P type ATPase; P1b ATPase; Thermophile

Indexed keywords

COPPER EXPORTING ADENOSINE TRIPHOSPHATASE;

EID: 33746750825     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.07.012     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Møller J.V., Juul B., and Le Maire M. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1286 (1996) 1-51
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 1-51
    • Møller, J.V.1    Juul, B.2    Le Maire, M.3
  • 2
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen K.B., and Palmgren M.G. Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46 (1998) 84-101
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 3
    • 33646830005 scopus 로고
    • Ion motive ATPases. I. Ubiquity, properties, and significance to cell function
    • Pedersen P.L., and Carafoli E. Ion motive ATPases. I. Ubiquity, properties, and significance to cell function. Trends Biochem. Sci. 12 (1987) 146-150
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 146-150
    • Pedersen, P.L.1    Carafoli, E.2
  • 4
    • 0032845338 scopus 로고    scopus 로고
    • Families of soft-metal-ion-transporting ATPases
    • Rensing C., Ghosh M., and Rosen B.P. Families of soft-metal-ion-transporting ATPases. J. Bacteriol. 181 (1999) 5891-5897
    • (1999) J. Bacteriol. , vol.181 , pp. 5891-5897
    • Rensing, C.1    Ghosh, M.2    Rosen, B.P.3
  • 5
    • 0034602290 scopus 로고    scopus 로고
    • Escherichia coli soft metal ion-translocating ATPases
    • Gatti D., Mitra B., and Rosen B.P. Escherichia coli soft metal ion-translocating ATPases. J. Biol. Chem. 275 (2000) 34009-34012
    • (2000) J. Biol. Chem. , vol.275 , pp. 34009-34012
    • Gatti, D.1    Mitra, B.2    Rosen, B.P.3
  • 6
    • 0031050483 scopus 로고    scopus 로고
    • Copper transport and its alterations in Menkes and Wilson diseases
    • DiDonato M., and Sarkar B. Copper transport and its alterations in Menkes and Wilson diseases. Biochim. Biophys. Acta 1360 (1997) 3-16
    • (1997) Biochim. Biophys. Acta , vol.1360 , pp. 3-16
    • DiDonato, M.1    Sarkar, B.2
  • 7
    • 0034703872 scopus 로고    scopus 로고
    • The Menkes copper transporter is required for the activation of tyrosinase
    • Petris M.J., Strausak D., and Mercer J.F. The Menkes copper transporter is required for the activation of tyrosinase. Hum. Mol. Genet. 9 (2000) 2845-2851
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2845-2851
    • Petris, M.J.1    Strausak, D.2    Mercer, J.F.3
  • 8
    • 0030199612 scopus 로고    scopus 로고
    • CPx-type ATPases: a class of P-type ATPases that pump heavy metals
    • Solioz M., and Vulpe C. CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21 (1996) 237-241
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 237-241
    • Solioz, M.1    Vulpe, C.2
  • 9
    • 0031974775 scopus 로고    scopus 로고
    • Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase
    • Gitschier J., Moffat B., Reilly D., Wood W.I., and Fairbrother W.J. Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nat. Struct. Biol. 5 (1998) 47-54
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 47-54
    • Gitschier, J.1    Moffat, B.2    Reilly, D.3    Wood, W.I.4    Fairbrother, W.J.5
  • 11
    • 0033529633 scopus 로고    scopus 로고
    • NMR structure and metal interactions of the CopZ copper chaperone
    • Wimmer R., Herrmann T., Solioz M., and Wuthrich K. NMR structure and metal interactions of the CopZ copper chaperone. J. Biol. Chem. 274 (1999) 22597-22603
    • (1999) J. Biol. Chem. , vol.274 , pp. 22597-22603
    • Wimmer, R.1    Herrmann, T.2    Solioz, M.3    Wuthrich, K.4
  • 12
    • 0030839796 scopus 로고    scopus 로고
    • N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat
    • Lutsenko S., Petrukhin K., Cooper M.J., Gilliam C.T., and Kaplan J.H. N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat. J. Biol. Chem. 272 (1997) 18939-18944
    • (1997) J. Biol. Chem. , vol.272 , pp. 18939-18944
    • Lutsenko, S.1    Petrukhin, K.2    Cooper, M.J.3    Gilliam, C.T.4    Kaplan, J.H.5
  • 13
    • 0031455381 scopus 로고    scopus 로고
    • Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B)
    • DiDonato M., Narindrasorasak S., Forbes J.R., Cox D.W., and Sarkar B. Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B). J. Biol. Chem. 272 (1997) 33279-33282
    • (1997) J. Biol. Chem. , vol.272 , pp. 33279-33282
    • DiDonato, M.1    Narindrasorasak, S.2    Forbes, J.R.3    Cox, D.W.4    Sarkar, B.5
  • 14
    • 0033568524 scopus 로고    scopus 로고
    • Expression, purification and copper-binding studies of the first metal-binding domain of Menkes protein
    • Jensen P.Y., Bonander N., Horn N., Tumer Z., and Farver O. Expression, purification and copper-binding studies of the first metal-binding domain of Menkes protein. Eur. J. Biochem. 264 (1999) 890-896
    • (1999) Eur. J. Biochem. , vol.264 , pp. 890-896
    • Jensen, P.Y.1    Bonander, N.2    Horn, N.3    Tumer, Z.4    Farver, O.5
  • 15
    • 2442572209 scopus 로고    scopus 로고
    • The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1
    • Walker J.M., Huster D., Ralle M., Morgan C.T., Blackburn N.J., and Lutsenko S. The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1. J. Biol. Chem. 279 (2004) 15376-15384
    • (2004) J. Biol. Chem. , vol.279 , pp. 15376-15384
    • Walker, J.M.1    Huster, D.2    Ralle, M.3    Morgan, C.T.4    Blackburn, N.J.5    Lutsenko, S.6
  • 16
    • 0027288228 scopus 로고
    • Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae
    • Odermatt A., Suter H., Krapf R., and Solioz M. Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem. 268 (1993) 12775-12779
    • (1993) J. Biol. Chem. , vol.268 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 17
    • 0142103656 scopus 로고    scopus 로고
    • Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain
    • Mana-Capelli S., Mandal A.K., and Arguello J.M. Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain. J. Biol. Chem. 278 (2003) 40534-40541
    • (2003) J. Biol. Chem. , vol.278 , pp. 40534-40541
    • Mana-Capelli, S.1    Mandal, A.K.2    Arguello, J.M.3
  • 18
    • 16344385272 scopus 로고    scopus 로고
    • Metal-binding characteristics of the amino-terminal domain of ZntA: binding of lead is different compared to cadmium and zinc
    • Liu J., Stemmler A.J., Fatima J., and Mitra B. Metal-binding characteristics of the amino-terminal domain of ZntA: binding of lead is different compared to cadmium and zinc. Biochemistry 44 (2005) 5159-5167
    • (2005) Biochemistry , vol.44 , pp. 5159-5167
    • Liu, J.1    Stemmler, A.J.2    Fatima, J.3    Mitra, B.4
  • 19
    • 0037033056 scopus 로고    scopus 로고
    • Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase
    • Fan B., and Rosen B.P. Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase. J. Biol. Chem. 277 (2002) 46987-46992
    • (2002) J. Biol. Chem. , vol.277 , pp. 46987-46992
    • Fan, B.1    Rosen, B.P.2
  • 20
    • 0037289803 scopus 로고    scopus 로고
    • Cd(2+) and the N-terminal metal-binding domain protect the putative membranous CPC motif of the Cd(2+)-ATPase of Listeria monocytogenes
    • Bal N., Wu C.C., Catty P., Guillain F., and Mintz E. Cd(2+) and the N-terminal metal-binding domain protect the putative membranous CPC motif of the Cd(2+)-ATPase of Listeria monocytogenes. Biochem. J. 369 (2003) 681-685
    • (2003) Biochem. J. , vol.369 , pp. 681-685
    • Bal, N.1    Wu, C.C.2    Catty, P.3    Guillain, F.4    Mintz, E.5
  • 21
    • 0141431021 scopus 로고    scopus 로고
    • Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA
    • Mandal A.K., and Arguello J.M. Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA. Biochemistry 42 (2003) 11040-11047
    • (2003) Biochemistry , vol.42 , pp. 11040-11047
    • Mandal, A.K.1    Arguello, J.M.2
  • 22
    • 0029664966 scopus 로고    scopus 로고
    • Phospholamban regulates the Ca2+-ATPase through intramembrane interactions
    • Kimura Y., Kurzdylowski K., Tada M., and MacLennan D.H. Phospholamban regulates the Ca2+-ATPase through intramembrane interactions. J. Biol. Chem. 271 (1996) 21726-21731
    • (1996) J. Biol. Chem. , vol.271 , pp. 21726-21731
    • Kimura, Y.1    Kurzdylowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 23
    • 0036510741 scopus 로고    scopus 로고
    • Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus
    • Mandal A.K., Cheung W.D., and Arguello J.M. Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus. J. Biol. Chem. 277 (2002) 7201-7208
    • (2002) J. Biol. Chem. , vol.277 , pp. 7201-7208
    • Mandal, A.K.1    Cheung, W.D.2    Arguello, J.M.3
  • 24
    • 0034635468 scopus 로고    scopus 로고
    • The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli
    • Sharma R., Rensing C., Rosen B.P., and Mitra B. The ATP hydrolytic activity of purified ZntA, a Pb(II)/Cd(II)/Zn(II)-translocating ATPase from Escherichia coli. J. Biol. Chem. 275 (2000) 3873-3878
    • (2000) J. Biol. Chem. , vol.275 , pp. 3873-3878
    • Sharma, R.1    Rensing, C.2    Rosen, B.P.3    Mitra, B.4
  • 25
    • 0035798632 scopus 로고    scopus 로고
    • Functional analysis of chimeric proteins of the Wilson Cu(I)-ATPase (ATP7B) and ZntA, a Pb(II)/Zn(II)/Cd(II)-ATPase from Escherichia coli
    • Hou Z.J., Narindrasorasak S., Bhushan B., Sarkar B., and Mitra B. Functional analysis of chimeric proteins of the Wilson Cu(I)-ATPase (ATP7B) and ZntA, a Pb(II)/Zn(II)/Cd(II)-ATPase from Escherichia coli. J. Biol. Chem. 276 (2001) 40858-40863
    • (2001) J. Biol. Chem. , vol.276 , pp. 40858-40863
    • Hou, Z.J.1    Narindrasorasak, S.2    Bhushan, B.3    Sarkar, B.4    Mitra, B.5
  • 26
    • 2942700106 scopus 로고    scopus 로고
    • A mutational study in the transmembrane domain of Ccc2p, the yeast Cu(I)-ATPase, shows different roles for each Cys-Pro-Cys cysteine
    • Lowe J., Vieyra A., Catty P., Guillain F., Mintz E., and Cuillel M. A mutational study in the transmembrane domain of Ccc2p, the yeast Cu(I)-ATPase, shows different roles for each Cys-Pro-Cys cysteine. J. Biol. Chem. 279 (2004) 25986-25994
    • (2004) J. Biol. Chem. , vol.279 , pp. 25986-25994
    • Lowe, J.1    Vieyra, A.2    Catty, P.3    Guillain, F.4    Mintz, E.5    Cuillel, M.6
  • 27
    • 0034804302 scopus 로고    scopus 로고
    • Purification and functional analysis of the copper ATPase CopA of Enterococcus hirae
    • Wunderli-Ye H., and Solioz M. Purification and functional analysis of the copper ATPase CopA of Enterococcus hirae. Biochem. Biophys. Res. Commun. 280 (2001) 713-719
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 713-719
    • Wunderli-Ye, H.1    Solioz, M.2
  • 28
    • 0037059855 scopus 로고    scopus 로고
    • Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells
    • Tsivkovskii R., Eisses J.F., Kaplan J.H., and Lutsenko S. Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells. J. Biol. Chem. 277 (2002) 976-983
    • (2002) J. Biol. Chem. , vol.277 , pp. 976-983
    • Tsivkovskii, R.1    Eisses, J.F.2    Kaplan, J.H.3    Lutsenko, S.4
  • 29
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase
    • Rae T.D., Schmidt P.J., Pufahl R.A., Culotta V.C., and O'Halloran T.V. Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284 (1999) 805-808
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 30
    • 0041856098 scopus 로고    scopus 로고
    • The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein
    • Huster D., and Lutsenko S. The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein. J. Biol. Chem. 278 (2003) 32212-32218
    • (2003) J. Biol. Chem. , vol.278 , pp. 32212-32218
    • Huster, D.1    Lutsenko, S.2
  • 31
    • 21244445058 scopus 로고    scopus 로고
    • Purification and functional reconstitution of the human Wilson copper ATPase, ATP7B
    • Portmann R., and Solioz M. Purification and functional reconstitution of the human Wilson copper ATPase, ATP7B. FEBS Lett. 579 (2005) 3589-3595
    • (2005) FEBS Lett. , vol.579 , pp. 3589-3595
    • Portmann, R.1    Solioz, M.2
  • 32
    • 0037035530 scopus 로고    scopus 로고
    • Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions
    • Cobine P.A., George G.N., Jones C.E., Wickramasinghe W.A., Solioz M., and Dameron C.T. Copper transfer from the Cu(I) chaperone, CopZ, to the repressor, Zn(II)CopY: metal coordination environments and protein interactions. Biochemistry 41 (2002) 5822-5829
    • (2002) Biochemistry , vol.41 , pp. 5822-5829
    • Cobine, P.A.1    George, G.N.2    Jones, C.E.3    Wickramasinghe, W.A.4    Solioz, M.5    Dameron, C.T.6
  • 33
    • 0035913995 scopus 로고    scopus 로고
    • Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance
    • Multhaup G., Strausak D., Bissig K.D., and Solioz M. Interaction of the CopZ copper chaperone with the CopA copper ATPase of Enterococcus hirae assessed by surface plasmon resonance. Biochem. Biophys. Res. Commun. 288 (2001) 172-177
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 172-177
    • Multhaup, G.1    Strausak, D.2    Bissig, K.D.3    Solioz, M.4
  • 34
    • 11144225837 scopus 로고    scopus 로고
    • Identification of the transmembrane metal binding site in Cu+-transporting PIB-type ATPases
    • Mandal A.K., Yang Y., Kertesz T.M., and Arguello J.M. Identification of the transmembrane metal binding site in Cu+-transporting PIB-type ATPases. J. Biol. Chem. 279 (2004) 54802-54807
    • (2004) J. Biol. Chem. , vol.279 , pp. 54802-54807
    • Mandal, A.K.1    Yang, Y.2    Kertesz, T.M.3    Arguello, J.M.4
  • 35
    • 0035958909 scopus 로고    scopus 로고
    • The regulation of catalytic activity of the Menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites
    • Voskoboinik I., Mar J., Strausak D., and Camakaris J. The regulation of catalytic activity of the Menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites. J. Biol. Chem. 276 (2001) 28620-28627
    • (2001) J. Biol. Chem. , vol.276 , pp. 28620-28627
    • Voskoboinik, I.1    Mar, J.2    Strausak, D.3    Camakaris, J.4
  • 36
    • 0035910261 scopus 로고    scopus 로고
    • The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner
    • Tsivkovskii R., MacArthur B.C., and Lutsenko S. The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner. J. Biol. Chem. 276 (2001) 2234-2242
    • (2001) J. Biol. Chem. , vol.276 , pp. 2234-2242
    • Tsivkovskii, R.1    MacArthur, B.C.2    Lutsenko, S.3
  • 37
    • 0025975040 scopus 로고
    • The calcium pumping ATPase of the plasma membrane
    • Carafoli E. The calcium pumping ATPase of the plasma membrane. Annu. Rev. Physiol. 53 (1991) 531-547
    • (1991) Annu. Rev. Physiol. , vol.53 , pp. 531-547
    • Carafoli, E.1
  • 38
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: protein structure, mechanism of action, and role in cardiac function
    • Simmerman H.K., and Jones L.R. Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol. Rev. 78 (1998) 921-947
    • (1998) Physiol. Rev. , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 39
    • 0034193428 scopus 로고    scopus 로고
    • The plant plasma membrane H(+)-ATPase: structure, function and regulation
    • Morsomme P., and Boutry M. The plant plasma membrane H(+)-ATPase: structure, function and regulation. Biochim. Biophys. Acta 1465 (2000) 1-16
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 1-16
    • Morsomme, P.1    Boutry, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.