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Volumn 169, Issue 3, 2010, Pages 406-412

Helical image reconstruction of the outward-open human erythrocyte band 3 membrane domain in tubular crystals

Author keywords

Band 3; Cryo electron microscopy; Iterative helical real space reconstruction; Membrane protein structure; Tubular crystal

Indexed keywords

ERYTHROCYTE BAND 3 PROTEIN;

EID: 76749162402     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.12.009     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 0020492242 scopus 로고
    • Evaluation of the structural interdependence of the membrane-spanning and cytoplasmic domains of band 3
    • Appell K.C., and Low P.S. Evaluation of the structural interdependence of the membrane-spanning and cytoplasmic domains of band 3. Biochemistry 21 (1982) 2151-2157
    • (1982) Biochemistry , vol.21 , pp. 2151-2157
    • Appell, K.C.1    Low, P.S.2
  • 2
    • 0018759156 scopus 로고
    • Anion transport in red blood cells. I. Chemical properties of anion recognition sites as revealed by structure-activity relationships of aromatic sulfonic acids
    • Barzilay M., Ship S., and Cabantchik Z.I. Anion transport in red blood cells. I. Chemical properties of anion recognition sites as revealed by structure-activity relationships of aromatic sulfonic acids. Membr. Biochem. 2 (1979) 227-254
    • (1979) Membr. Biochem. , vol.2 , pp. 227-254
    • Barzilay, M.1    Ship, S.2    Cabantchik, Z.I.3
  • 3
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity
    • Casey J.R., and Reithmeier R.A. Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity. J. Biol. Chem. 266 (1991) 15726-15737
    • (1991) J. Biol. Chem. , vol.266 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.2
  • 4
    • 0032452006 scopus 로고    scopus 로고
    • Anion exchangers in the red cell and beyond
    • Casey J.R., and Reithmeier R.A. Anion exchangers in the red cell and beyond. Biochem. Cell Biol. 76 (1998) 709-713
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 709-713
    • Casey, J.R.1    Reithmeier, R.A.2
  • 5
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85 (2000) 225-234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 6
    • 33845305513 scopus 로고    scopus 로고
    • The iterative helical real space reconstruction method, surmounting the problems posed by real polymers
    • Egelman E.H. The iterative helical real space reconstruction method, surmounting the problems posed by real polymers. J. Struct. Biol. 157 (2007) 83-94
    • (2007) J. Struct. Biol. , vol.157 , pp. 83-94
    • Egelman, E.H.1
  • 7
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB, processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., and Leith A. SPIDER and WEB, processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116 (1996) 190-199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 8
    • 0033525686 scopus 로고    scopus 로고
    • Topology of the membrane domain of human erythrocyte anion exchange protein, AE1
    • Fujinaga J., Tang X.B., and Casey J.R. Topology of the membrane domain of human erythrocyte anion exchange protein, AE1. J. Biol. Chem. 274 (1999) 6626-6633
    • (1999) J. Biol. Chem. , vol.274 , pp. 6626-6633
    • Fujinaga, J.1    Tang, X.B.2    Casey, J.R.3
  • 9
    • 0021266827 scopus 로고
    • 2DIDS. Evidence for two conformations of the transport site of the human erythrocyte anion exchange protein
    • 2DIDS. Evidence for two conformations of the transport site of the human erythrocyte anion exchange protein. J. Gen. Physiol. 83 (1984) 657-681
    • (1984) J. Gen. Physiol. , vol.83 , pp. 657-681
    • Furuya, W.1    Tarshis, T.2    Law, F.Y.3    Knauf, P.A.4
  • 10
    • 0033572646 scopus 로고    scopus 로고
    • Structural model for the organization of the transmembrane spans of the human red-cell anion exchanger (band 3; AE1)
    • Groves J.D., and Tanner M.J. Structural model for the organization of the transmembrane spans of the human red-cell anion exchanger (band 3; AE1). Biochem. J. 344 (1999) 699-711
    • (1999) Biochem. J. , vol.344 , pp. 699-711
    • Groves, J.D.1    Tanner, M.J.2
  • 11
    • 0018638065 scopus 로고
    • Asymmetry in the mechanism for anion exchange in human red blood cell membranes. Evidence for reciprocating sites that react with one transported anion at a time
    • Gunn R.B., and Fröhlich O. Asymmetry in the mechanism for anion exchange in human red blood cell membranes. Evidence for reciprocating sites that react with one transported anion at a time. J. Gen. Physiol. 74 (1979) 351-374
    • (1979) J. Gen. Physiol. , vol.74 , pp. 351-374
    • Gunn, R.B.1    Fröhlich, O.2
  • 12
    • 0030860847 scopus 로고    scopus 로고
    • Proteolytic cleavage sites of band 3 protein in alkali-treated membranes, fidelity of hydropathy prediction for band 3 protein
    • Hamasaki N., Okubo K., Kuma H., Kang D., and Yae Y. Proteolytic cleavage sites of band 3 protein in alkali-treated membranes, fidelity of hydropathy prediction for band 3 protein. J. Biochem. 122 (1997) 577-585
    • (1997) J. Biochem. , vol.122 , pp. 577-585
    • Hamasaki, N.1    Okubo, K.2    Kuma, H.3    Kang, D.4    Yae, Y.5
  • 13
    • 0032461894 scopus 로고    scopus 로고
    • A new concept in polytopic membrane proteins following from the study of band 3 protein
    • Hamasaki N., Kuma H., Ota K., Sakaguchi M., and Mihara K. A new concept in polytopic membrane proteins following from the study of band 3 protein. Biochem. Cell Biol. 76 (1998) 729-733
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 729-733
    • Hamasaki, N.1    Kuma, H.2    Ota, K.3    Sakaguchi, M.4    Mihara, K.5
  • 14
    • 0018746219 scopus 로고
    • Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4′-diisothiocyano dihydrostilmen-2′2-disulfonate
    • Jennings M.L., and Passow H. Anion transport across the erythrocyte membrane, in situ proteolysis of band 3 protein, and cross-linking of proteolytic fragments by 4,4′-diisothiocyano dihydrostilmen-2′2-disulfonate. Biochim. Biophys. Acta 554 (1979) 498-519
    • (1979) Biochim. Biophys. Acta , vol.554 , pp. 498-519
    • Jennings, M.L.1    Passow, H.2
  • 15
    • 0026760577 scopus 로고
    • A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment
    • Kang D., Okubo K., Hamasaki N., Kuroda N., and Shiraki H. A structural study of the membrane domain of band 3 by tryptic digestion. Conformational change of band 3 in situ induced by alkali treatment. J. Biol. Chem. 267 (1992) 19211-19217
    • (1992) J. Biol. Chem. , vol.267 , pp. 19211-19217
    • Kang, D.1    Okubo, K.2    Hamasaki, N.3    Kuroda, N.4    Shiraki, H.5
  • 16
    • 77957092777 scopus 로고
    • Erythrocyte anion exchange and the band 3 protein, transport kinetics and molecular structure
    • Knauf P.A. Erythrocyte anion exchange and the band 3 protein, transport kinetics and molecular structure. Curr. Top. Membr. Transp. 12 (1979) 249-363
    • (1979) Curr. Top. Membr. Transp. , vol.12 , pp. 249-363
    • Knauf, P.A.1
  • 17
    • 0037066082 scopus 로고    scopus 로고
    • Topology of the anion exchange protein AE1, the controversial sidedness of lysine 743
    • Kuma H., Shinde A.A., Howren T.R., and Jennings M.L. Topology of the anion exchange protein AE1, the controversial sidedness of lysine 743. Biochemistry 41 (2002) 3380-3388
    • (2002) Biochemistry , vol.41 , pp. 3380-3388
    • Kuma, H.1    Shinde, A.A.2    Howren, T.R.3    Jennings, M.L.4
  • 18
    • 0037066128 scopus 로고    scopus 로고
    • Molecular basis and functional consequences of the dominant effects of the mutant band 3 on the structure of normal band 3 in Southeast Asian ovalocytosis
    • Kuma H., Abe Y., Askin D., Bruce L.J., Hamasaki T., Tanner M.J., and Hamasaki N. Molecular basis and functional consequences of the dominant effects of the mutant band 3 on the structure of normal band 3 in Southeast Asian ovalocytosis. Biochemistry 41 (2002) 3311-3320
    • (2002) Biochemistry , vol.41 , pp. 3311-3320
    • Kuma, H.1    Abe, Y.2    Askin, D.3    Bruce, L.J.4    Hamasaki, T.5    Tanner, M.J.6    Hamasaki, N.7
  • 19
    • 0017202108 scopus 로고
    • Effects of incorporated trypsin on anion exchange and membrane proteins in human red blood cell ghost
    • Lepke S., and Passow H. Effects of incorporated trypsin on anion exchange and membrane proteins in human red blood cell ghost. Biochim. Biophys. Acta 455 (1976) 353-370
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 353-370
    • Lepke, S.1    Passow, H.2
  • 20
    • 0026545038 scopus 로고
    • Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis
    • Lepke S., Becker A., and Passow H. Mediation of inorganic anion transport by the hydrophobic domain of mouse erythroid band 3 protein expressed in oocytes of Xenopus laevis. Biochim. Biophys. Acta 1106 (1992) 13-16
    • (1992) Biochim. Biophys. Acta , vol.1106 , pp. 13-16
    • Lepke, S.1    Becker, A.2    Passow, H.3
  • 21
    • 0023726261 scopus 로고
    • Localization of the carboxyl terminus of band 3 to the cytoplasmic side of the erythrocyte membrane using antibodies raised against a synthetic peptide
    • Lieberman D.M., and Reithmeier R.A. Localization of the carboxyl terminus of band 3 to the cytoplasmic side of the erythrocyte membrane using antibodies raised against a synthetic peptide. J. Biol. Chem. 263 (1988) 10022-10028
    • (1988) J. Biol. Chem. , vol.263 , pp. 10022-10028
    • Lieberman, D.M.1    Reithmeier, R.A.2
  • 22
    • 0026063047 scopus 로고
    • Monomeric erythrocyte band 3 protein transports anions
    • Lindenthal S., and Schubert D. Monomeric erythrocyte band 3 protein transports anions. Proc. Natl. Acad. Sci. USA 88 (1991) 6540-6544
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6540-6544
    • Lindenthal, S.1    Schubert, D.2
  • 23
    • 0022922389 scopus 로고
    • Structure and function of the cytoplasmic domain of band 3, center of erythrocyte membrane-peripheral protein interactions
    • Low P.S. Structure and function of the cytoplasmic domain of band 3, center of erythrocyte membrane-peripheral protein interactions. Biochim. Biophys. Acta 864 (1986) 145-167
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 145-167
    • Low, P.S.1
  • 24
    • 0033377664 scopus 로고    scopus 로고
    • EMAN, semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN, semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 25
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell J.A., and Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142 (2003) 334-347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 26
    • 0029616179 scopus 로고
    • A structural study of the carboxyl terminal region of the human erythrocyte band 3 protein
    • Mori A., Okubo K., Kang D., and Hamasaki N. A structural study of the carboxyl terminal region of the human erythrocyte band 3 protein. J. Biochem. 118 (1995) 1192-1198
    • (1995) J. Biochem. , vol.118 , pp. 1192-1198
    • Mori, A.1    Okubo, K.2    Kang, D.3    Hamasaki, N.4
  • 27
    • 0028006541 scopus 로고
    • Red blood cell band 3. Lysine 539 and lysine 851 react with the sameH2DIDS (4,4′-diisothiocyanodihydrostilbene- 2,2′-disulfonic acid) molecule
    • Okubo K., Kang D., Hamasaki N., and Jennings M.L. Red blood cell band 3. Lysine 539 and lysine 851 react with the sameH2DIDS (4,4′-diisothiocyanodihydrostilbene- 2,2′-disulfonic acid) molecule. J. Biol. Chem. 269 (1994) 1918-1926
    • (1994) J. Biol. Chem. , vol.269 , pp. 1918-1926
    • Okubo, K.1    Kang, D.2    Hamasaki, N.3    Jennings, M.L.4
  • 28
    • 0022615649 scopus 로고
    • Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane
    • Passow H. Molecular aspects of band 3 protein-mediated anion transport across the red blood cell membrane. Rev. Physiol. Biochem. Pharmacol. 103 (1986) 61-203
    • (1986) Rev. Physiol. Biochem. Pharmacol. , vol.103 , pp. 61-203
    • Passow, H.1
  • 30
    • 33845305824 scopus 로고    scopus 로고
    • Application of the iterative helical real-space reconstruction method to large membranous tubular crystals of P-type ATPases
    • Pomfret A.J., Rice W.J., and Stokes D.L. Application of the iterative helical real-space reconstruction method to large membranous tubular crystals of P-type ATPases. J. Struct. Biol. 157 (2007) 106-116
    • (2007) J. Struct. Biol. , vol.157 , pp. 106-116
    • Pomfret, A.J.1    Rice, W.J.2    Stokes, D.L.3
  • 31
    • 0030745799 scopus 로고    scopus 로고
    • Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3
    • Popov M., Tam L.Y., Li J., and Reithmeier R.A. Mapping the ends of transmembrane segments in a polytopic membrane protein. Scanning N-glycosylation mutagenesis of extracytosolic loops in the anion exchanger, band 3. J. Biol. Chem. 272 (1997) 18325-18332
    • (1997) J. Biol. Chem. , vol.272 , pp. 18325-18332
    • Popov, M.1    Tam, L.Y.2    Li, J.3    Reithmeier, R.A.4
  • 32
    • 0033561328 scopus 로고    scopus 로고
    • Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined by scanning and insertional N-glycosylation mutagenesis
    • Popov M., Li J., and Reithmeier R.A. Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined by scanning and insertional N-glycosylation mutagenesis. Biochem. J. 339 (1998) 269-279
    • (1998) Biochem. J. , vol.339 , pp. 269-279
    • Popov, M.1    Li, J.2    Reithmeier, R.A.3
  • 34
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens, a fresh look at tobacco mosaic virus
    • Sachse C., Chen J.Z., Coureux P.D., Stroupe M.E., Fändrich M., and Grigorieff N. High-resolution electron microscopy of helical specimens, a fresh look at tobacco mosaic virus. J. Mol. Biol. 371 (2007) 812-835
    • (2007) J. Mol. Biol. , vol.371 , pp. 812-835
    • Sachse, C.1    Chen, J.Z.2    Coureux, P.D.3    Stroupe, M.E.4    Fändrich, M.5    Grigorieff, N.6
  • 35
    • 0017801444 scopus 로고
    • - transport site of human red blood cells by kinetic analysis of the inhibitory effects of a chemical probe
    • - transport site of human red blood cells by kinetic analysis of the inhibitory effects of a chemical probe. Biochim. Biophys. Acta 508 (1978) 357-363
    • (1978) Biochim. Biophys. Acta , vol.508 , pp. 357-363
    • Shami, Y.1    Rothstein, A.2    Knauf, P.A.3
  • 36
    • 0001420610 scopus 로고
    • Computer image processing of electron micrographs of biological structures with helical symmetry
    • Stewart M. Computer image processing of electron micrographs of biological structures with helical symmetry. J. Electron. Microsc. Tech. 9 (1988) 325-358
    • (1988) J. Electron. Microsc. Tech. , vol.9 , pp. 325-358
    • Stewart, M.1
  • 38
    • 33745738625 scopus 로고    scopus 로고
    • The functional role of arginine 901 at the C-terminus of the human anion transporter band 3 protein
    • Takazaki S., Abe Y., Kang D., Li C., Jin X., Ueda T., and Hamasaki N. The functional role of arginine 901 at the C-terminus of the human anion transporter band 3 protein. J. Biochem. 139 (2006) 903-912
    • (2006) J. Biochem. , vol.139 , pp. 903-912
    • Takazaki, S.1    Abe, Y.2    Kang, D.3    Li, C.4    Jin, X.5    Ueda, T.6    Hamasaki, N.7
  • 39
    • 0031466796 scopus 로고    scopus 로고
    • The structure and function of band 3 (AE1), recent developments
    • Tanner M.J. The structure and function of band 3 (AE1), recent developments. Mol. Membr. Biol. 14 (1997) 155-165
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 155-165
    • Tanner, M.J.1
  • 40
    • 0024511767 scopus 로고
    • Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus of the protein to the cytoplasmic side of the red cell membrane and distribution of the protein in some human tissues
    • Wainwright S.D., Tanner M.J., Martin G.E., Yendle J.E., and Holmes C. Monoclonal antibodies to the membrane domain of the human erythrocyte anion transport protein. Localization of the C-terminus of the protein to the cytoplasmic side of the red cell membrane and distribution of the protein in some human tissues. Biochem. J. 258 (1989) 211-220
    • (1989) Biochem. J. , vol.258 , pp. 211-220
    • Wainwright, S.D.1    Tanner, M.J.2    Martin, G.E.3    Yendle, J.E.4    Holmes, C.5
  • 41
    • 0028339981 scopus 로고
    • Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, band 3
    • Wang D.N., Sarabia V.E., Reithmeier R.A., and Kühlbrandt W. Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, band 3. EMBO J. 13 (1994) 3230-3235
    • (1994) EMBO J. , vol.13 , pp. 3230-3235
    • Wang, D.N.1    Sarabia, V.E.2    Reithmeier, R.A.3    Kühlbrandt, W.4
  • 42
    • 0034329189 scopus 로고    scopus 로고
    • Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
    • Zhang D., Kiyatkin A., Bolin J.T., and Low P.S. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 96 (2000) 2925-2933
    • (2000) Blood , vol.96 , pp. 2925-2933
    • Zhang, D.1    Kiyatkin, A.2    Bolin, J.T.3    Low, P.S.4
  • 43
    • 0037474222 scopus 로고    scopus 로고
    • Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1
    • Zhu Q., Lee D.W., and Casey J.R. Novel topology in C-terminal region of the human plasma membrane anion exchanger, AE1. J. Biol. Chem. 278 (2003) 3112-3120
    • (2003) J. Biol. Chem. , vol.278 , pp. 3112-3120
    • Zhu, Q.1    Lee, D.W.2    Casey, J.R.3


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