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Volumn 162, Issue 2, 2008, Pages 219-228

Structural analysis of 2D crystals of gastric H+,K+-ATPase in different states of the transport cycle

Author keywords

2D crystal; Cryo EM; Gastric proton pump; H+,K+ ATPase; P type ATPase

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (POTASSIUM); FLUOROALUMINATE; GLYCOPROTEIN E1; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; NUCLEOTIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; TRYPSIN;

EID: 42649116079     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2007.12.005     Document Type: Article
Times cited : (13)

References (54)
  • 3
    • 0025191377 scopus 로고
    • Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology
    • Chabre M. Aluminofluoride and beryllofluoride complexes: a new phosphate analogs in enzymology. Trends Biochem. Sci. 15 (1990) 6-10
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 6-10
    • Chabre, M.1
  • 6
    • 0023874147 scopus 로고
    • A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: application to lens ATPases
    • Chifflet S., Torriglia A., Chiesa R., and Tolosa S. A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: application to lens ATPases. Anal. Biochem. 168 (1988) 1-4
    • (1988) Anal. Biochem. , vol.168 , pp. 1-4
    • Chifflet, S.1    Torriglia, A.2    Chiesa, R.3    Tolosa, S.4
  • 7
    • 0029137474 scopus 로고
    • Functional significance of the beta-subunit for heterodimeric P-type ATPases
    • Chow D.C., and Forte J.G. Functional significance of the beta-subunit for heterodimeric P-type ATPases. J. Exp. Biol. 198 (1995) 1-17
    • (1995) J. Exp. Biol. , vol.198 , pp. 1-17
    • Chow, D.C.1    Forte, J.G.2
  • 12
    • 0343052627 scopus 로고    scopus 로고
    • A spectral estimation approach to contrast transfer function detection in electron microscopy
    • Fernandez J.J., Sanjurjo J.R., and Carazo J.M. A spectral estimation approach to contrast transfer function detection in electron microscopy. Ultramicroscopy 68 (1997) 267-295
    • (1997) Ultramicroscopy , vol.68 , pp. 267-295
    • Fernandez, J.J.1    Sanjurjo, J.R.2    Carazo, J.M.3
  • 13
    • 0031700068 scopus 로고    scopus 로고
    • The structural study of membrane proteins by electron crystallography
    • Fujiyoshi Y. The structural study of membrane proteins by electron crystallography. Adv. Biophys. 35 (1998) 25-80
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 17
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution
    • Henderson R., Baldwin J., Downing K., Lepault J., and Zemiln F. Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 19 (1986) 147-178
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.2    Downing, K.3    Lepault, J.4    Zemiln, F.5
  • 18
    • 0028888879 scopus 로고
    • Gastric acid secretion
    • Hersey S.J., and Sachs G. Gastric acid secretion. Physiol. Rev. 75 (1995) 155-189
    • (1995) Physiol. Rev. , vol.75 , pp. 155-189
    • Hersey, S.J.1    Sachs, G.2
  • 19
    • 0032695274 scopus 로고    scopus 로고
    • Trehalose embedding technique for high-resolution electron crystallography: application to structural study on bacteriorhodopsin
    • Hirai T., Murata K., Mitsuoka K., Kimura Y., and Fujiyoshi Y. Trehalose embedding technique for high-resolution electron crystallography: application to structural study on bacteriorhodopsin. J. Electron Microsc. (Tokyo) 48 (1999) 653-658
    • (1999) J. Electron Microsc. (Tokyo) , vol.48 , pp. 653-658
    • Hirai, T.1    Murata, K.2    Mitsuoka, K.3    Kimura, Y.4    Fujiyoshi, Y.5
  • 20
    • 33745762313 scopus 로고    scopus 로고
    • Modulatory and catalytic modes of ATP binding by the calcium pump
    • Jensen A.M., Sørensen T.L., Olesen C., Møller J.V., and Nissen P. Modulatory and catalytic modes of ATP binding by the calcium pump. EMBO J. 25 (2006) 2305-2314
    • (2006) EMBO J. , vol.25 , pp. 2305-2314
    • Jensen, A.M.1    Sørensen, T.L.2    Olesen, C.3    Møller, J.V.4    Nissen, P.5
  • 22
    • 0038621773 scopus 로고    scopus 로고
    • Structure and mechanism of Na,K-ATPase: functional sites and their interactions
    • Jørgensen P.L., Hakansson K.O., and Karlish S.J. Structure and mechanism of Na,K-ATPase: functional sites and their interactions. Annu. Rev. Physiol. 65 (2003) 817-849
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 817-849
    • Jørgensen, P.L.1    Hakansson, K.O.2    Karlish, S.J.3
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crys. 24 (1991) 946-950
    • (1991) J. Appl. Crys. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • Kühlbrandt W. Biology, structure and mechanism of P-type ATPases. Nat. Rev. Mol. Cell Biol. 5 (2004) 282-295
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 282-295
    • Kühlbrandt, W.1
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0037672768 scopus 로고    scopus 로고
    • The biochemistry and physiology of metallic fluoride: action, mechanism, and implications
    • Li L. The biochemistry and physiology of metallic fluoride: action, mechanism, and implications. Crit. Rev. Oral. Biol. Med. 14 (2003) 100-114
    • (2003) Crit. Rev. Oral. Biol. Med. , vol.14 , pp. 100-114
    • Li, L.1
  • 29
    • 16844381593 scopus 로고    scopus 로고
    • Inhibitor and ion binding sites on the gastric H,K-ATPase
    • Munson K., Garcia R., and Sachs G. Inhibitor and ion binding sites on the gastric H,K-ATPase. Biochemistry 44 (2005) 5267-5284
    • (2005) Biochemistry , vol.44 , pp. 5267-5284
    • Munson, K.1    Garcia, R.2    Sachs, G.3
  • 30
    • 0031595675 scopus 로고    scopus 로고
    • 2+ pump of sarcoplasmic reticulum: a view along the lipid bilayer at 9-Å resolution
    • 2+ pump of sarcoplasmic reticulum: a view along the lipid bilayer at 9-Å resolution. Biophys. J. 75 (1998) 41-52
    • (1998) Biophys. J. , vol.75 , pp. 41-52
    • Ogawa, H.1    Stokes, D.L.2    Sasabe, H.3    Toyoshima, C.4
  • 31
    • 11144330054 scopus 로고    scopus 로고
    • Dephosphorylation of the calcium pump coupled to counterion occlusion
    • Olesen C., Sørensen T.L., Nielsen R.C., Møller J.V., and Nissen P. Dephosphorylation of the calcium pump coupled to counterion occlusion. Science 306 (2004) 2251-2255
    • (2004) Science , vol.306 , pp. 2251-2255
    • Olesen, C.1    Sørensen, T.L.2    Nielsen, R.C.3    Møller, J.V.4    Nissen, P.5
  • 34
    • 0015867369 scopus 로고
    • Evidence for an aspartyl phosphate residue at the active site of sodium and potassium ion transport adenosine triphosphatase
    • Post R.L., and Kume S. Evidence for an aspartyl phosphate residue at the active site of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 248 (1973) 6993-7000
    • (1973) J. Biol. Chem. , vol.248 , pp. 6993-7000
    • Post, R.L.1    Kume, S.2
  • 35
    • 85025408146 scopus 로고
    • Flexibility of an active center in sodium-plus-potassium adenosine triphosphatase
    • Post R.L., Kume S., Tobin T., Orcutt B., and Sen A.K. Flexibility of an active center in sodium-plus-potassium adenosine triphosphatase. J. Gen. Physiol. 54 (1969) 306S-326S
    • (1969) J. Gen. Physiol. , vol.54
    • Post, R.L.1    Kume, S.2    Tobin, T.3    Orcutt, B.4    Sen, A.K.5
  • 36
  • 38
    • 0025321011 scopus 로고
    • The mechanism and structure of the gastric H,K-ATPase
    • Rabon E.C., and Reuben M.A. The mechanism and structure of the gastric H,K-ATPase. Annu. Rev. Physiol. 52 (1990) 321-344
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 321-344
    • Rabon, E.C.1    Reuben, M.A.2
  • 43
    • 2942668632 scopus 로고    scopus 로고
    • Phosphoryl transfer and calcium ion occlusion in the calcium pump
    • Sørensen T.L., Møller J.V., and Nissen P. Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science 304 (2004) 1672-1675
    • (2004) Science , vol.304 , pp. 1672-1675
    • Sørensen, T.L.1    Møller, J.V.2    Nissen, P.3
  • 44
    • 0030250308 scopus 로고    scopus 로고
    • A set of computer programs for determining defocus and astigmatism in electron images
    • Tani K., Sasabe H., and Toyoshima C. A set of computer programs for determining defocus and astigmatism in electron images. Ultramicroscopy 65 (1996) 31-44
    • (1996) Ultramicroscopy , vol.65 , pp. 31-44
    • Tani, K.1    Sasabe, H.2    Toyoshima, C.3
  • 45
    • 0020491101 scopus 로고
    • +)-ATPase modified with N-[p-(2-benzimidazolyl)phenyl]maleimide
    • +)-ATPase modified with N-[p-(2-benzimidazolyl)phenyl]maleimide. J. Biol. Chem. 257 (1982) 10659-10667
    • (1982) J. Biol. Chem. , vol.257 , pp. 10659-10667
    • Taniguchi, K.1    Suzuki, K.2    Iida, S.3
  • 46
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima C., and Nomura H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418 (2002) 605-611
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 47
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima C., and Mizutani T. Crystal structure of the calcium pump with a bound ATP analogue. Nature 430 (2004) 529-535
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 49
    • 9244232176 scopus 로고    scopus 로고
    • Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima C., Nomura H., and Tsuda T. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432 (2004) 361-368
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 50
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima C., Nakasako M., Nomura H., and Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405 (2000) 647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 52
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin N. Acetylcholine receptor channel imaged in the open state. Nature 373 (1995) 37-43
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 53
    • 0030907484 scopus 로고    scopus 로고
    • Three-dimensional structure of the porcine gastric H,K-ATPase from negatively stained crystals
    • Xian Y., and Hebert H. Three-dimensional structure of the porcine gastric H,K-ATPase from negatively stained crystals. J. Struct. Biol. 118 (1997) 169-177
    • (1997) J. Struct. Biol. , vol.118 , pp. 169-177
    • Xian, Y.1    Hebert, H.2
  • 54
    • 0025413443 scopus 로고
    • SDS purification of porcine H,K-ATPase from gastric mucosa
    • Yeh L.A., Cosgrove P., and Holt W.F. SDS purification of porcine H,K-ATPase from gastric mucosa. Membr. Biochem. 9 (1990) 129-140
    • (1990) Membr. Biochem. , vol.9 , pp. 129-140
    • Yeh, L.A.1    Cosgrove, P.2    Holt, W.F.3


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