메뉴 건너뛰기




Volumn 170, Issue 1, 2010, Pages 60-68

Structural and functional characterization of H+,K+-ATPase with bound fluorinated phosphate analogs

Author keywords

Cryo electron microscopy; H+,K+ ATPase; Membrane protein structure; P type ATPase; Two dimensional crystal

Indexed keywords

HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; MAGNESIUM ION; POTASSIUM ION; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 77950518814     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.12.008     Document Type: Article
Times cited : (24)

References (34)
  • 1
  • 2
    • 0021104435 scopus 로고
    • A least-squares method for determining structure factors in three-dimensional tilted-view reconstructions
    • Agard D.A. A least-squares method for determining structure factors in three-dimensional tilted-view reconstructions. J. Mol. Biol. 1983, 167:849-852.
    • (1983) J. Mol. Biol. , vol.167 , pp. 849-852
    • Agard, D.A.1
  • 3
    • 0023426241 scopus 로고
    • Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the gamma phosphate of GTP
    • Bigay J., Deterre P., Pfister C., Chabre M. Fluoride complexes of aluminium or beryllium act on G-proteins as reversibly bound analogues of the gamma phosphate of GTP. EMBO J. 1987, 6:2907-2913.
    • (1987) EMBO J. , vol.6 , pp. 2907-2913
    • Bigay, J.1    Deterre, P.2    Pfister, C.3    Chabre, M.4
  • 4
    • 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., 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. 1988, 168:1-4.
    • (1988) Anal. Biochem. , vol.168 , pp. 1-4
    • Chifflet, S.1    Torriglia, A.2    Chiesa, R.3    Tolosa, S.4
  • 5
    • 0029137474 scopus 로고
    • Functional significance of the beta-subunit for heterodimeric P-type ATPases
    • Chow D.C., Forte J.G. Functional significance of the beta-subunit for heterodimeric P-type ATPases. J. Exp. Biol. 1995, 198:1-17.
    • (1995) J. Exp. Biol. , vol.198 , pp. 1-17
    • Chow, D.C.1    Forte, J.G.2
  • 7
    • 2442504897 scopus 로고    scopus 로고
    • 2+-ATPase: changes in catalytic and transport sites during phosphoenzyme hydrolysis
    • 2+-ATPase: changes in catalytic and transport sites during phosphoenzyme hydrolysis. J. Biol. Chem. 2004, 279:14991-14998.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14991-14998
    • Danko, S.1    Yamasaki, K.2    Daiho, T.3    Suzuki, H.4
  • 8
    • 69249093401 scopus 로고    scopus 로고
    • 2+ by beryllium fluoride: structural changes during phosphorylation and isomerization
    • 2+ by beryllium fluoride: structural changes during phosphorylation and isomerization. J. Biol. Chem. 2009, 284:22722-22735.
    • (2009) J. Biol. Chem. , vol.284 , pp. 22722-22735
    • Danko, S.1    Daiho, T.2    Yamasaki, K.3    Liu, X.4    Suzuki, H.5
  • 10
    • 67749135743 scopus 로고    scopus 로고
    • E2P-state stabilization by the N-terminal tail of the H,K-ATPase β-subunit is critical for efficient proton pumping under in vivo conditions
    • Dürr K.L., Abe K., Tavraz N.N., Friedrich T. E2P-state stabilization by the N-terminal tail of the H,K-ATPase β-subunit is critical for efficient proton pumping under in vivo conditions. J. Biol. Chem. 2009, 284:20147-20154.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20147-20154
    • Dürr, K.L.1    Abe, K.2    Tavraz, N.N.3    Friedrich, T.4
  • 11
    • 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. 1998, 35:25-80.
    • (1998) Adv. Biophys. , vol.35 , pp. 25-80
    • Fujiyoshi, Y.1
  • 13
    • 0015935494 scopus 로고
    • +-stimulated ATPase in purified microsomes of bullfrog oxynic cells
    • +-stimulated ATPase in purified microsomes of bullfrog oxynic cells. Biochim. Biophys. Acta 1973, 307:169-180.
    • (1973) Biochim. Biophys. Acta , vol.307 , pp. 169-180
    • Ganser, A.L.1    Forte, J.G.2
  • 14
    • 1942521362 scopus 로고    scopus 로고
    • Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique
    • Gyobu N., Tani K., Hiroaki Y., Kamegawa A., Mitsuoka K., Fujiyoshi Y. Improved specimen preparation for cryo-electron microscopy using a symmetric carbon sandwich technique. J. Struct. Biol. 2004, 146:325-333.
    • (2004) J. Struct. Biol. , vol.146 , pp. 325-333
    • Gyobu, N.1    Tani, K.2    Hiroaki, Y.3    Kamegawa, A.4    Mitsuoka, K.5    Fujiyoshi, Y.6
  • 16
    • 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., Zemiln F. Structure of purple membrane from Halobacterium halobium: recording, measurement and evaluation of electron micrographs at 3.5 Å resolution. Ultramicroscopy 1986, 19:147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.2    Downing, K.3    Lepault, J.4    Zemiln, F.5
  • 18
    • 0027236527 scopus 로고
    • An essential role for the extracellular domain of the sodium-potassium-ATPase β-subunit in cation occlusion
    • Lutsenko S., Kaplan J.H. An essential role for the extracellular domain of the sodium-potassium-ATPase β-subunit in cation occlusion. Biochemistry 1993, 32:6737-6743.
    • (1993) Biochemistry , vol.32 , pp. 6737-6743
    • Lutsenko, S.1    Kaplan, J.H.2
  • 24
    • 0015867369 scopus 로고
    • Evidence for an aspartyl phosphate residue at the active site of sodium and potassium ion transport adenosine triphosphatase
    • Post R.L., Kume S. Evidence for an aspartyl phosphate residue at the active site of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 1973, 248:6993-7000.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6993-7000
    • Post, R.L.1    Kume, S.2
  • 25
    • 0025321011 scopus 로고
    • The mechanism and structure of the gastric H,K-ATPase
    • Rabon E.C., Reuben M.A. The mechanism and structure of the gastric H,K-ATPase. Annu. Rev. Physiol. 1990, 52:321-344.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 321-344
    • Rabon, E.C.1    Reuben, M.A.2
  • 28
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4 Å resolution
    • Shinoda T., Ogawa H., Cornelius F., Toyoshima C. Crystal structure of the sodium-potassium pump at 2.4 Å resolution. Nature 2009, 459:446-450.
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 29
    • 0030250308 scopus 로고    scopus 로고
    • A set of computer programs for determining defocus and astigmatism in electron images
    • Tani K., Sasabe H., Toyoshima C. A set of computer programs for determining defocus and astigmatism in electron images. Ultramicroscopy 1996, 65:31-44.
    • (1996) Ultramicroscopy , vol.65 , pp. 31-44
    • Tani, K.1    Sasabe, H.2    Toyoshima, C.3
  • 30
    • 9244232176 scopus 로고    scopus 로고
    • Luminal gating mechanism revealed in calcium pump crystal structures with phosphate analogues
    • Toyoshima C., Nomura H., Tsuda T. Luminal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 2004, 432:361-368.
    • (2004) Nature , vol.432 , pp. 361-368
    • Toyoshima, C.1    Nomura, H.2    Tsuda, T.3
  • 31
    • 38049138584 scopus 로고    scopus 로고
    • How processing of aspartylphosphate is coupled to luminal gating of the ion pathway in the calcium pump
    • Toyoshima C., Norimatsu Y., Iwasawa S., Tsuda T., Ogawa H. How processing of aspartylphosphate is coupled to luminal gating of the ion pathway in the calcium pump. Proc. Nat. Acad. Sci. USA 2007, 104:19831-19836.
    • (2007) Proc. Nat. Acad. Sci. USA , vol.104 , pp. 19831-19836
    • Toyoshima, C.1    Norimatsu, Y.2    Iwasawa, S.3    Tsuda, T.4    Ogawa, H.5
  • 32
    • 0036424944 scopus 로고    scopus 로고
    • Novel three-dimensional variant of the watershed transform for segmentation of electron density maps
    • Volkmann N.A. Novel three-dimensional variant of the watershed transform for segmentation of electron density maps. J. Struct. Biol. 2002, 138:123-129.
    • (2002) J. Struct. Biol. , vol.138 , pp. 123-129
    • Volkmann, N.A.1
  • 33
    • 0021984713 scopus 로고
    • +-ATPase-rich vesicles: implications for HCl secretion and parietal cell physiology
    • +-ATPase-rich vesicles: implications for HCl secretion and parietal cell physiology. Am. J. Physiol. 1985, 248:G595-G607.
    • (1985) Am. J. Physiol. , vol.248
    • Wolosin, J.M.1
  • 34
    • 0025413443 scopus 로고
    • SDS purification of porcine H,K-ATPase from gastric mucosa
    • Yen L.A., Cosgrove P., Holt W. SDS purification of porcine H,K-ATPase from gastric mucosa. Membr. Biochem. 1990, 9:129-140.
    • (1990) Membr. Biochem. , vol.9 , pp. 129-140
    • Yen, L.A.1    Cosgrove, P.2    Holt, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.