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Volumn 350, Issue 5, 2005, Pages 997-1016

Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore

Author keywords

Cholera; Membrane protein crystallization; Pore forming toxins; Vibrio cholerae cytolysin; X ray crystallography

Indexed keywords

BACTERIAL TOXIN; CELL SURFACE RECEPTOR; CYTOLYSIN; LIPOSOME; OCTYL GLUCOSIDE; OLIGOMER;

EID: 21744447839     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.045     Document Type: Article
Times cited : (112)

References (83)
  • 1
    • 0029004327 scopus 로고
    • Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin
    • A. Zitzer, I. Walev, M. Palmer, and S. Bhakdi Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin Med. Microbiol. Immunol. (Berl.) 184 1995 37 44
    • (1995) Med. Microbiol. Immunol. (Berl.) , vol.184 , pp. 37-44
    • Zitzer, A.1    Walev, I.2    Palmer, M.3    Bhakdi, S.4
  • 2
    • 0030900285 scopus 로고    scopus 로고
    • Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells
    • A. Zitzer, T.M. Wassenaar, I. Walev, and S. Bhakdi Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells Infect. Immun. 65 1997 1293 1298
    • (1997) Infect. Immun. , vol.65 , pp. 1293-1298
    • Zitzer, A.1    Wassenaar, T.M.2    Walev, I.3    Bhakdi, S.4
  • 4
    • 0025331048 scopus 로고
    • The cytolysin gene of Vibrio vulnificus: Sequence and relationship to the Vibrio cholerae E1 Tor hemolysin gene
    • K. Yamamoto, A.C. Wright, J.B. Kaper, and J.G. Morris Jr The cytolysin gene of Vibrio vulnificus: sequence and relationship to the Vibrio cholerae E1 Tor hemolysin gene Infect. Immun. 58 1990 2706 2709
    • (1990) Infect. Immun. , vol.58 , pp. 2706-2709
    • Yamamoto, K.1    Wright, A.C.2    Kaper, J.B.3    Morris Jr., J.G.4
  • 5
    • 0021718292 scopus 로고
    • Cloning of the structural gene (hly) for the haemolysin of Vibrio cholerae El Tor strain 017
    • P.A. Manning, M.H. Brown, and M.W. Heuzenroeder Cloning of the structural gene (hly) for the haemolysin of Vibrio cholerae El Tor strain 017 Gene 31 1984 225 231
    • (1984) Gene , vol.31 , pp. 225-231
    • Manning, P.A.1    Brown, M.H.2    Heuzenroeder, M.W.3
  • 6
    • 0025609753 scopus 로고
    • Two-step processing for activation of the cytolysin/hemolysin of Vibrio cholerae O1 biotype El Tor: Nucleotide sequence of the structural gene (hlyA) and characterization of the processed products
    • K. Yamamoto, Y. Ichinose, H. Shinagawa, K. Makino, A. Nakata, and M. Iwanaga Two-step processing for activation of the cytolysin/hemolysin of Vibrio cholerae O1 biotype El Tor: nucleotide sequence of the structural gene (hlyA) and characterization of the processed products Infect. Immun. 58 1990 4106 4116
    • (1990) Infect. Immun. , vol.58 , pp. 4106-4116
    • Yamamoto, K.1    Ichinose, Y.2    Shinagawa, H.3    Makino, K.4    Nakata, A.5    Iwanaga, M.6
  • 7
    • 0025121520 scopus 로고
    • Vibrio cholerae HlyA hemolysin is processed by proteolysis
    • R.H. Hall, and B.S. Drasar Vibrio cholerae HlyA hemolysin is processed by proteolysis Infect. Immun. 58 1990 3375 3379
    • (1990) Infect. Immun. , vol.58 , pp. 3375-3379
    • Hall, R.H.1    Drasar, B.S.2
  • 8
    • 0029858955 scopus 로고    scopus 로고
    • In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases
    • K. Nagamune, K. Yamamoto, A. Naka, J. Matsuyama, T. Miwatani, and T. Honda In vitro proteolytic processing and activation of the recombinant precursor of El Tor cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases Infect. Immun. 64 1996 4655 4658
    • (1996) Infect. Immun. , vol.64 , pp. 4655-4658
    • Nagamune, K.1    Yamamoto, K.2    Naka, A.3    Matsuyama, J.4    Miwatani, T.5    Honda, T.6
  • 10
    • 0031024004 scopus 로고    scopus 로고
    • Intramolecular chaperone activity of the pro-region of Vibrio cholerae El Tor cytolysin
    • K. Nagamune, K. Yamamoto, and T. Honda Intramolecular chaperone activity of the pro-region of Vibrio cholerae El Tor cytolysin J. Biol. Chem. 272 1997 1338 1343
    • (1997) J. Biol. Chem. , vol.272 , pp. 1338-1343
    • Nagamune, K.1    Yamamoto, K.2    Honda, T.3
  • 11
    • 0037302443 scopus 로고    scopus 로고
    • Vibrio cholerae cytolysin is composed of an α-hemolysin-like core
    • R. Olson, and E. Gouaux Vibrio cholerae cytolysin is composed of an α-hemolysin-like core Protein Sci. 12 2003 379 383
    • (2003) Protein Sci. , vol.12 , pp. 379-383
    • Olson, R.1    Gouaux, E.2
  • 12
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • R. Olson, H. Nariya, K. Yokota, Y. Kamio, and E. Gouaux Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel Nature Struct. Biol. 6 1999 134 140
    • (1999) Nature Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 13
    • 0033103175 scopus 로고    scopus 로고
    • The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins
    • J.D. Pedelacq, L. Maveyraud, G. Prévost, L. Baba-Moussa, A. Gonzalez, and E. Courcelle The structure of a Staphylococcus aureus leucocidin component (LukF-PV) reveals the fold of the water-soluble species of a family of transmembrane pore-forming toxins Struct. Fold. Des. 7 1999 277 287
    • (1999) Struct. Fold. Des. , vol.7 , pp. 277-287
    • Pedelacq, J.D.1    Maveyraud, L.2    Prévost, G.3    Baba-Moussa, L.4    Gonzalez, A.5    Courcelle, E.6
  • 14
    • 4644355909 scopus 로고    scopus 로고
    • Crystal structure of leucotoxin S component: New insight into the Staphylococcal beta-barrel pore-forming toxins
    • V. Guillet, P. Roblin, S. Werner, M. Coraiola, G. Menestrina, and H. Monteil Crystal structure of leucotoxin S component: new insight into the Staphylococcal beta-barrel pore-forming toxins J. Biol. Chem. 279 2004 41028 41037
    • (2004) J. Biol. Chem. , vol.279 , pp. 41028-41037
    • Guillet, V.1    Roblin, P.2    Werner, S.3    Coraiola, M.4    Menestrina, G.5    Monteil, H.6
  • 15
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • L. Song, M.R. Hobaugh, C. Shustak, S. Cheley, H. Bayley, and J.E. Gouaux Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore Science 274 1996 1859 1866
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 16
    • 0037427958 scopus 로고    scopus 로고
    • β-Barrel membrane protein folding and structure viewed through the lens of α-hemolysin
    • M. Montoya, and E. Gouaux β-Barrel membrane protein folding and structure viewed through the lens of α-hemolysin Biochim. Biophys. Acta 1609 2003 19 27
    • (2003) Biochim. Biophys. Acta , vol.1609 , pp. 19-27
    • Montoya, M.1    Gouaux, E.2
  • 17
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis
    • B. Walker, M. Krishnasastry, L. Zorn, and H. Bayley Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis J. Biol. Chem. 267 1992 21782 21786
    • (1992) J. Biol. Chem. , vol.267 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 18
    • 0043234285 scopus 로고    scopus 로고
    • Assembly and topography of the prepore complex in cholesterol-dependent cytolysins
    • A.P. Heuck, R.K. Tweten, and A.E. Johnson Assembly and topography of the prepore complex in cholesterol-dependent cytolysins J. Biol. Chem. 278 2003 31218 31225
    • (2003) J. Biol. Chem. , vol.278 , pp. 31218-31225
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 20
    • 0033543208 scopus 로고    scopus 로고
    • Anthrax protective antigen: Prepore-to-pore conversion
    • C.J. Miller, J.L. Elliott, and R.J. Collier Anthrax protective antigen: prepore-to-pore conversion Biochemistry 38 1999 10432 10441
    • (1999) Biochemistry , vol.38 , pp. 10432-10441
    • Miller, C.J.1    Elliott, J.L.2    Collier, R.J.3
  • 21
    • 0035909809 scopus 로고    scopus 로고
    • Packing is a key selection factor in the evolution of protein hydrophobic cores
    • J. Chen, and W.E. Stites Packing is a key selection factor in the evolution of protein hydrophobic cores Biochemistry 40 2001 15280 15289
    • (2001) Biochemistry , vol.40 , pp. 15280-15289
    • Chen, J.1    Stites, W.E.2
  • 22
    • 0030037293 scopus 로고    scopus 로고
    • Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1
    • H. Ikigai, A. Akatsuka, H. Tsujiyama, T. Nakae, and T. Shimamura Mechanism of membrane damage by El Tor hemolysin of Vibrio cholerae O1 Infect. Immun. 64 1996 2968 2973
    • (1996) Infect. Immun. , vol.64 , pp. 2968-2973
    • Ikigai, H.1    Akatsuka, A.2    Tsujiyama, H.3    Nakae, T.4    Shimamura, T.5
  • 23
    • 0033556418 scopus 로고    scopus 로고
    • Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane
    • A. Zitzer, O. Zitzer, S. Bhakdi, and M. Palmer Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane J. Biol. Chem. 274 1999 1375 1380
    • (1999) J. Biol. Chem. , vol.274 , pp. 1375-1380
    • Zitzer, A.1    Zitzer, O.2    Bhakdi, S.3    Palmer, M.4
  • 24
    • 0036432233 scopus 로고    scopus 로고
    • Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: A TEM study
    • J. Robin Harris, S. Bhakdi, U. Meissner, D. Scheffler, R. Bittman, and G. Li Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: a TEM study J. Struct. Biol. 139 2002 122 135
    • (2002) J. Struct. Biol. , vol.139 , pp. 122-135
    • Robin Harris, J.1    Bhakdi, S.2    Meissner, U.3    Scheffler, D.4    Bittman, R.5    Li, G.6
  • 25
    • 0034694978 scopus 로고    scopus 로고
    • Vibrio cholerae cytolysin: Assembly and membrane insertion of the oligomeric pore are tightly linked and are not detectably restricted by membrane fluidity
    • A. Zitzer, J.R. Harris, S.E. Kemminer, O. Zitzer, S. Bhakdi, J. Muething, and M. Palmer Vibrio cholerae cytolysin: assembly and membrane insertion of the oligomeric pore are tightly linked and are not detectably restricted by membrane fluidity Biochim. Biophys. Acta 1509 2000 264 274
    • (2000) Biochim. Biophys. Acta , vol.1509 , pp. 264-274
    • Zitzer, A.1    Harris, J.R.2    Kemminer, S.E.3    Zitzer, O.4    Bhakdi, S.5    Muething, J.6    Palmer, M.7
  • 26
    • 0029741086 scopus 로고    scopus 로고
    • HlyA hemolysin of Vibrio cholerae O1 biotype E1 Tor. Identification of the hemolytic complex and evidence for the formation of anion-selective ion-permeable channels
    • K. Menzl, E. Maier, T. Chakraborty, and R. Benz HlyA hemolysin of Vibrio cholerae O1 biotype E1 Tor. Identification of the hemolytic complex and evidence for the formation of anion-selective ion-permeable channels Eur. J. Biochem. 240 1996 646 654
    • (1996) Eur. J. Biochem. , vol.240 , pp. 646-654
    • Menzl, K.1    Maier, E.2    Chakraborty, T.3    Benz, R.4
  • 28
    • 0030793119 scopus 로고    scopus 로고
    • Mode of primary binding to target membranes and pore formation induced by Vibrio cholerae cytolysin (hemolysin)
    • A. Zitzer, M. Palmer, U. Weller, T. Wassenaar, C. Biermann, J. Tranum-Jensen, and S. Bhakdi Mode of primary binding to target membranes and pore formation induced by Vibrio cholerae cytolysin (hemolysin) Eur. J. Biochem. 247 1997 209 216
    • (1997) Eur. J. Biochem. , vol.247 , pp. 209-216
    • Zitzer, A.1    Palmer, M.2    Weller, U.3    Wassenaar, T.4    Biermann, C.5    Tranum-Jensen, J.6    Bhakdi, S.7
  • 29
    • 0031017025 scopus 로고    scopus 로고
    • Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle
    • N. Saha, and K.K. Banerjee Carbohydrate-mediated regulation of interaction of Vibrio cholerae hemolysin with erythrocyte and phospholipid vesicle J. Biol. Chem. 272 1997 162 167
    • (1997) J. Biol. Chem. , vol.272 , pp. 162-167
    • Saha, N.1    Banerjee, K.K.2
  • 30
    • 0032850956 scopus 로고    scopus 로고
    • Analysis of receptor for Vibrio cholerae El tor hemolysin with a monoclonal antibody that recognizes glycophorin B of human erythrocyte membrane
    • D. Zhang, J. Takahashi, T. Seno, Y. Tani, and T. Honda Analysis of receptor for Vibrio cholerae El tor hemolysin with a monoclonal antibody that recognizes glycophorin B of human erythrocyte membrane Infect. Immun. 67 1999 5332 5337
    • (1999) Infect. Immun. , vol.67 , pp. 5332-5337
    • Zhang, D.1    Takahashi, J.2    Seno, T.3    Tani, Y.4    Honda, T.5
  • 32
    • 0023091105 scopus 로고
    • Structure and evolution of ricin B chain
    • E. Rutenber, M. Ready, and J.D. Robertus Structure and evolution of ricin B chain Nature 326 1987 624 626
    • (1987) Nature , vol.326 , pp. 624-626
    • Rutenber, E.1    Ready, M.2    Robertus, J.D.3
  • 33
    • 0032922393 scopus 로고    scopus 로고
    • Two forms of Vibrio cholerae O1 El Tor hemolysin derived from identical precursor protein
    • H. Ikigai, T. Ono, T. Nakae, H. Otsuru, and T. Shimamura Two forms of Vibrio cholerae O1 El Tor hemolysin derived from identical precursor protein Biochim. Biophys. Acta 1415 1999 297 305
    • (1999) Biochim. Biophys. Acta , vol.1415 , pp. 297-305
    • Ikigai, H.1    Ono, T.2    Nakae, T.3    Otsuru, H.4    Shimamura, T.5
  • 34
    • 0026217133 scopus 로고
    • Nucleotide sequence and expression of an extracellular hemolysin gene of Aeromonas hydrophila
    • I. Hirono, and T. Aoki Nucleotide sequence and expression of an extracellular hemolysin gene of Aeromonas hydrophila Microb. Pathog. 11 1991 189 197
    • (1991) Microb. Pathog. , vol.11 , pp. 189-197
    • Hirono, I.1    Aoki, T.2
  • 35
    • 0031889115 scopus 로고    scopus 로고
    • Inactivation of two haemolytic toxin genes in Aeromonas hydrophila attenuates virulence in a suckling mouse model
    • C.Y. Wong, M.W. Heuzenroeder, and R.L. Flower Inactivation of two haemolytic toxin genes in Aeromonas hydrophila attenuates virulence in a suckling mouse model Microbiology 144 1998 291 298
    • (1998) Microbiology , vol.144 , pp. 291-298
    • Wong, C.Y.1    Heuzenroeder, M.W.2    Flower, R.L.3
  • 36
    • 0027742414 scopus 로고
    • Cloning and characterization of three hemolysin genes from Aeromonas salmonicida
    • I. Hirono, and T. Aoki Cloning and characterization of three hemolysin genes from Aeromonas salmonicida Microb. Pathog. 15 1993 269 282
    • (1993) Microb. Pathog. , vol.15 , pp. 269-282
    • Hirono, I.1    Aoki, T.2
  • 37
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • P.H. Bessette, F. Åslund, J. Beckwith, and G. Georgiou Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm Proc. Natl Acad. Sci. USA 96 1999 13703 13708
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Åslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 38
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • W.A. Hendrickson, J.R. Horton, and D.M. LeMaster Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure EMBO J. 9 1990 1665 1672
    • (1990) EMBO J. , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    Lemaster, D.M.3
  • 39
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • W.A. Hendrickson Determination of macromolecular structures from anomalous diffraction of synchrotron radiation Science 254 1991 51 58
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 40
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 41
  • 42
    • 0028158628 scopus 로고
    • PHD - An automatic mail server for protein secondary structure prediction
    • B. Rost, C. Sander, and R. Schneider PHD - an automatic mail server for protein secondary structure prediction Comput. Appl. Biosci. 10 1994 53 60
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 45
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • G. Kleywegt Use of non-crystallographic symmetry in protein structure refinement Acta Crystallog. sect. D 52 1996 842 857
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 842-857
    • Kleywegt, G.1
  • 46
    • 0029125825 scopus 로고
    • Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal α-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • B. Walker, and H. Bayley Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal α-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification J. Biol. Chem. 270 1995 23065 23071
    • (1995) J. Biol. Chem. , vol.270 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 48
    • 0032993061 scopus 로고    scopus 로고
    • A functional protein pore with a "retro" transmembrane domain
    • S. Cheley, O. Braha, X. Lu, S. Conlan, and H. Bayley A functional protein pore with a "retro" transmembrane domain Protein Sci. 8 1999 1257 1267
    • (1999) Protein Sci. , vol.8 , pp. 1257-1267
    • Cheley, S.1    Braha, O.2    Lu, X.3    Conlan, S.4    Bayley, H.5
  • 50
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • R. Loris Principles of structures of animal and plant lectins Biochim. Biophys. Acta 1572 2002 198 208
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 51
    • 0016174105 scopus 로고
    • Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-Å resolution
    • R.M. Sweet, H.T. Wright, J. Janin, C.H. Chothia, and D.M. Blow Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-Å resolution Biochemistry 13 1974 4212 4228
    • (1974) Biochemistry , vol.13 , pp. 4212-4228
    • Sweet, R.M.1    Wright, H.T.2    Janin, J.3    Chothia, C.H.4    Blow, D.M.5
  • 53
    • 0034599596 scopus 로고    scopus 로고
    • Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand
    • Y. Liu, A.J. Chirino, Z. Misulovin, C. Leteux, T. Feizi, M.C. Nussenzweig, and P.J. Bjorkman Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand J. Expt. Med. 191 2000 1105 1116
    • (2000) J. Expt. Med. , vol.191 , pp. 1105-1116
    • Liu, Y.1    Chirino, A.J.2    Misulovin, Z.3    Leteux, C.4    Feizi, T.5    Nussenzweig, M.C.6    Bjorkman, P.J.7
  • 54
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • L. Holm, and C. Sander Protein structure comparison by alignment of distance matrices J. Mol. Biol. 233 1993 123 138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 55
    • 0032513154 scopus 로고    scopus 로고
    • Structure of the complex of Maclura pomifera agglutinin and the T-antigen disaccharide, Galβ1,3GalNAc
    • X. Lee, A. Thompson, Z. Zhang, H. Ton-that, J. Biesterfeldt, and C. Ogata Structure of the complex of Maclura pomifera agglutinin and the T-antigen disaccharide, Galβ1,3GalNAc J. Biol. Chem. 273 1998 6312 6318
    • (1998) J. Biol. Chem. , vol.273 , pp. 6312-6318
    • Lee, X.1    Thompson, A.2    Zhang, Z.3    Ton-That, H.4    Biesterfeldt, J.5    Ogata, C.6
  • 58
    • 0034980642 scopus 로고    scopus 로고
    • Structure of Cry2Aa suggests an unexpected receptor binding epitope
    • R.J. Morse, T. Yamamoto, and R.M. Stroud Structure of Cry2Aa suggests an unexpected receptor binding epitope Structure (Camb) 9 2001 409 417
    • (2001) Structure (Camb) , vol.9 , pp. 409-417
    • Morse, R.J.1    Yamamoto, T.2    Stroud, R.M.3
  • 59
    • 0037093547 scopus 로고    scopus 로고
    • Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose
    • Y. Bourne, C.H. Astoul, V. Zamboni, W.J. Peumans, L. Menu-Bouaouiche, and E.J. Van Damme Structural basis for the unusual carbohydrate-binding specificity of jacalin towards galactose and mannose Biochem. J. 364 2002 173 180
    • (2002) Biochem. J. , vol.364 , pp. 173-180
    • Bourne, Y.1    Astoul, C.H.2    Zamboni, V.3    Peumans, W.J.4    Menu-Bouaouiche, L.5    Van Damme, E.J.6
  • 62
    • 0031058884 scopus 로고    scopus 로고
    • Rotation function calculations with GLRF program
    • L. Tong, and M.G. Rossmann Rotation function calculations with GLRF program Methods Enzymol. 276 1997 594 611
    • (1997) Methods Enzymol. , vol.276 , pp. 594-611
    • Tong, L.1    Rossmann, M.G.2
  • 63
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • N. Naslavsky, R. Stein, A. Yanai, G. Friedlander, and A. Taraboulos Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform J. Biol. Chem. 272 1997 6324 6331
    • (1997) J. Biol. Chem. , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 65
    • 4544239246 scopus 로고    scopus 로고
    • Ostreolysin, a pore-forming protein from the oyster mushroom, interacts specifically with membrane cholesterol-rich lipid domains
    • K. Sepcic, S. Berne, K. Rebolj, U. Batista, A. Plemenitas, M. Sentjurc, and P. Macek Ostreolysin, a pore-forming protein from the oyster mushroom, interacts specifically with membrane cholesterol-rich lipid domains FEBS Letters 575 2004 81 85
    • (2004) FEBS Letters , vol.575 , pp. 81-85
    • Sepcic, K.1    Berne, S.2    Rebolj, K.3    Batista, U.4    Plemenitas, A.5    Sentjurc, M.6    MacEk, P.7
  • 66
    • 0037134485 scopus 로고    scopus 로고
    • Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation
    • M. Zhuang, D.I. Oltean, I. Gomez, A.K. Pullikuth, M. Soberon, A. Bravo, and S.S. Gill Heliothis virescens and Manduca sexta lipid rafts are involved in Cry1A toxin binding to the midgut epithelium and subsequent pore formation J. Biol. Chem. 277 2002 13863 13872
    • (2002) J. Biol. Chem. , vol.277 , pp. 13863-13872
    • Zhuang, M.1    Oltean, D.I.2    Gomez, I.3    Pullikuth, A.K.4    Soberon, M.5    Bravo, A.6    Gill, S.S.7
  • 67
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • P. Sheffield, S. Garrard, and Z. Derewenda Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors Protein Expr. Purif. 15 1999 34 39
    • (1999) Protein Expr. Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 68
    • 0034846215 scopus 로고    scopus 로고
    • Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems
    • S.A. Guerrero, H.J. Hecht, B. Hofmann, H. Biebl, and M. Singh Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems Appl. Microbiol. Biotechnol. 56 2001 718 723
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 718-723
    • Guerrero, S.A.1    Hecht, H.J.2    Hofmann, B.3    Biebl, H.4    Singh, M.5
  • 69
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 70
    • 0037407011 scopus 로고    scopus 로고
    • Arresting and releasing staphylococcal α-hemolysin at intermediate stages of pore formation by engineered disulfide bonds
    • T. Kawate, and E. Gouaux Arresting and releasing staphylococcal α-hemolysin at intermediate stages of pore formation by engineered disulfide bonds Protein Sci. 12 2003 997 1006
    • (2003) Protein Sci. , vol.12 , pp. 997-1006
    • Kawate, T.1    Gouaux, E.2
  • 71
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter R.M. Sweet Academic Press New York
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter R.M. Sweet Methods in Enzymology vol. 276 1997 Academic Press New York
    • (1997) Methods in Enzymology , vol.276
    • Otwinowski, Z.1    Minor, W.2
  • 73
    • 0033229974 scopus 로고    scopus 로고
    • Reciprocal-space solvent flattening
    • T.C. Terwilliger Reciprocal-space solvent flattening Acta Crystallog. sect. D 55 1999 1863 1871
    • (1999) Acta Crystallog. Sect. D , vol.55 , pp. 1863-1871
    • Terwilliger, T.C.1
  • 74
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • T.C. Terwilliger Maximum-likelihood density modification Acta Crystallog. sect. D 56 2000 965 972
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 75
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • A. Jones, and M. Kjeldgaard Electron-density map interpretation Methods Enzymol. 277 1997 173 208
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, A.1    Kjeldgaard, M.2
  • 77
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • M.L. Johnson, J.J. Correia, D.A. Yphantis, and H.R. Halvorson Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques Biophys. J. 36 1981 575 588
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 78
    • 0017917637 scopus 로고
    • Determination of partial specific volumes for lipid-associated proteins
    • J.C. Steele Jr, C. Tanford, and J.A. Reynolds Determination of partial specific volumes for lipid-associated proteins Methods Enzymol. 48 1978 11 23
    • (1978) Methods Enzymol. , vol.48 , pp. 11-23
    • Steele Jr., J.C.1    Tanford, C.2    Reynolds, J.A.3
  • 79
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • R.M. Esnouf Further additions to MolScript version 1.4, including reading and contouring of electron-density maps Acta Crystallog. D 55 1999 938 940
    • (1999) Acta Crystallog. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 80
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 81
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • P. Gouet, E. Courcelle, D.I. Stuart, and F. Métoz ESPript: analysis of multiple sequence alignments in PostScript Bioinformatics 15 1999 305 308
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4
  • 82
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 22 1994 4673 4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 83
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch
    • B. Walker, O. Braha, S. Cheley, and H. Bayley An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch Chem. Biol. 2 1995 99 105
    • (1995) Chem. Biol. , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4


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