메뉴 건너뛰기




Volumn 290, Issue 21, 2015, Pages 13191-13201

X-ray and cryo-electron microscopy structures of Monalysin pore-forming toxin reveal multimerization of the pro-form

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ELECTRON MICROSCOPES; ELECTRON MICROSCOPY; LIGHT SCATTERING; METABOLITES; OLIGOMERS; PEPTIDES; TOXIC MATERIALS;

EID: 84930227238     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.646109     Document Type: Article
Times cited : (23)

References (49)
  • 1
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: From structure to function
    • Parker, M. W., and Feil, S. C. (2005) Pore-forming protein toxins: from structure to function. Prog. Biophys. Mol. Biol. 88, 91-142
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 2
    • 0030865151 scopus 로고    scopus 로고
    • Channel-forming toxins: Tales of transformation
    • Gouaux, E. (1997) Channel-forming toxins: tales of transformation. Curr. Opin. Struct. Biol. 7, 566-573
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 566-573
    • Gouaux, E.1
  • 3
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J. E. (1996) Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore. Science 274, 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
  • 4
    • 0034695613 scopus 로고    scopus 로고
    • E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy
    • Wallace, A. J., Stillman, T. J., Atkins, A., Jamieson, S. J., Bullough, P. A., Green, J., and Artymiuk, P. J. (2000) E. coli hemolysin E (HlyE, ClyA, SheA): x-ray crystal structure of the toxin and observation of membrane pores by electron microscopy. Cell 100, 265-276
    • (2000) Cell , vol.100 , pp. 265-276
    • Wallace, A.J.1    Stillman, T.J.2    Atkins, A.3    Jamieson, S.J.4    Bullough, P.A.5    Green, J.6    Artymiuk, P.J.7
  • 5
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism
    • Mueller, M., Grauschopf, U., Maier, T., Glockshuber, R., and Ban, N. (2009) The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism. Nature 459, 726-730
    • (2009) Nature , vol.459 , pp. 726-730
    • Mueller, M.1    Grauschopf, U.2    Maier, T.3    Glockshuber, R.4    Ban, N.5
  • 6
    • 79956294243 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins
    • De, S., and Olson, R. (2011) Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins. Proc. Natl. Acad. Sci. U.S.A. 108, 7385-7390
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 7385-7390
    • De, S.1    Olson, R.2
  • 7
    • 21744447839 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore
    • Olson, R., and Gouaux, E. (2005) Crystal structure of the Vibrio cholerae cytolysin (VCC) pro-toxin and its assembly into a heptameric transmembrane pore. J. Mol. Biol. 350, 997-1016
    • (2005) J. Mol. Biol. , vol.350 , pp. 997-1016
    • Olson, R.1    Gouaux, E.2
  • 8
    • 0032932083 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel
    • Olson, R., Nariya, H., Yokota, K., Kamio, Y., and Gouaux, E. (1999) Crystal structure of staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat. Struct. Biol. 6, 134-140
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 9
    • 40549092995 scopus 로고    scopus 로고
    • A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of β-barrel pore-forming toxins
    • Roblin, P., Guillet, V., Joubert, O., Keller, D., Erard, M., Maveyraud, L., Prévost, G., and Mourey, L. (2008) A covalent S-F heterodimer of leucotoxin reveals molecular plasticity of β-barrel pore-forming toxins. Proteins 71, 485-496
    • (2008) Proteins , vol.71 , pp. 485-496
    • Roblin, P.1    Guillet, V.2    Joubert, O.3    Keller, D.4    Erard, M.5    Maveyraud, L.6    Prévost, G.7    Mourey, L.8
  • 10
    • 80054794259 scopus 로고    scopus 로고
    • Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components
    • Yamashita, K., Kawai, Y., Tanaka, Y., Hirano, N., Kaneko, J., Tomita, N., Ohta, M., Kamio, Y., Yao, M., and Tanaka, I. (2011) Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components. Proc. Natl. Acad. Sci. U.S.A. 108, 17314-17319
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 17314-17319
    • Yamashita, K.1    Kawai, Y.2    Tanaka, Y.3    Hirano, N.4    Kaneko, J.5    Tomita, N.6    Ohta, M.7    Kamio, Y.8    Yao, M.9    Tanaka, I.10
  • 13
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy, S. S., Bresnahan, P. A., Leppla, S. H., Klimpel, K. R., and Thomas, G. (1992) Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 267, 16396-16402
    • (1992) J. Biol. Chem. , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 14
    • 0028018856 scopus 로고
    • Anthrax protective antigen forms oligomers during intoxication of mammalian cells
    • Milne, J. C., Furlong, D., Hanna, P. C., Wall, J. S., and Collier, R. J. (1994) Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269, 20607-20612
    • (1994) J. Biol. Chem. , vol.269 , pp. 20607-20612
    • Milne, J.C.1    Furlong, D.2    Hanna, P.C.3    Wall, J.S.4    Collier, R.J.5
  • 15
    • 0032539990 scopus 로고    scopus 로고
    • Identification of residues lining the anthrax protective antigen channel
    • Benson, E. L., Huynh, P. D., Finkelstein, A., and Collier, R. J. (1998) Identification of residues lining the anthrax protective antigen channel. Biochemistry 37, 3941-3948
    • (1998) Biochemistry , vol.37 , pp. 3941-3948
    • Benson, E.L.1    Huynh, P.D.2    Finkelstein, A.3    Collier, R.J.4
  • 16
    • 4444267311 scopus 로고    scopus 로고
    • Structure of heptameric protective antigen bound to an anthrax toxin receptor: A role for receptor in pH-dependent pore formation
    • Lacy, D. B., Wigelsworth, D. J., Melnyk, R. A., Harrison, S. C., and Collier, R. J. (2004) Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation. Proc. Natl. Acad. Sci. U.S.A. 101, 13147-13151
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13147-13151
    • Lacy, D.B.1    Wigelsworth, D.J.2    Melnyk, R.A.3    Harrison, S.C.4    Collier, R.J.5
  • 17
    • 0027275474 scopus 로고
    • Dimerization stabilizes the pore-forming toxin aerolysin in solution
    • van der Goot, F. G., Ausio, J., Wong, K. R., Pattus, F., and Buckley, J. T. (1993) Dimerization stabilizes the pore-forming toxin aerolysin in solution. J. Biol. Chem. 268, 18272-18279
    • (1993) J. Biol. Chem. , vol.268 , pp. 18272-18279
    • Van Der Goot, F.G.1    Ausio, J.2    Wong, K.R.3    Pattus, F.4    Buckley, J.T.5
  • 18
    • 0028044180 scopus 로고
    • Partial purification of the rat erythrocyte receptor for the channel-forming toxin aerolysin and reconstitution into planar lipid bilayers
    • Gruber, H. J., Wilmsen, H. U., Cowell, S., Schindler, H., and Buckley, J. T. (1994) Partial purification of the rat erythrocyte receptor for the channel-forming toxin aerolysin and reconstitution into planar lipid bilayers. Mol. Microbiol. 14, 1093-1101
    • (1994) Mol. Microbiol. , vol.14 , pp. 1093-1101
    • Gruber, H.J.1    Wilmsen, H.U.2    Cowell, S.3    Schindler, H.4    Buckley, J.T.5
  • 19
    • 0028077896 scopus 로고
    • The C-terminal peptide produced upon proteolytic activation of the cytolytic toxin aerolysin is not involved in channel formation
    • van der Goot, F. G., Hardie, K. R., Parker, M. W., and Buckley, J. T. (1994) The C-terminal peptide produced upon proteolytic activation of the cytolytic toxin aerolysin is not involved in channel formation. J. Biol. Chem. 269, 30496-30501
    • (1994) J. Biol. Chem. , vol.269 , pp. 30496-30501
    • Van Der Goot, F.G.1    Hardie, K.R.2    Parker, M.W.3    Buckley, J.T.4
  • 20
    • 0030660558 scopus 로고    scopus 로고
    • Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel
    • Cabiaux, V., Buckley, J. T., Wattiez, R., Ruysschaert, J. M., Parker, M. W., and van der Goot, F. G. (1997) Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel. Biochemistry 36, 15224-15232
    • (1997) Biochemistry , vol.36 , pp. 15224-15232
    • Cabiaux, V.1    Buckley, J.T.2    Wattiez, R.3    Ruysschaert, J.M.4    Parker, M.W.5    Van Der Goot, F.G.6
  • 21
    • 79960941170 scopus 로고    scopus 로고
    • Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin
    • Iacovache, I., Degiacomi, M. T., Pernot, L., Ho, S., Schiltz, M., Dal Peraro, M., and van der Goot, F. G. (2011) Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin. PLoS Pathog. 7, e1002135
    • (2011) PLoS Pathog. , vol.7 , pp. e1002135
    • Iacovache, I.1    Degiacomi, M.T.2    Pernot, L.3    Ho, S.4    Schiltz, M.5    Dal Peraro, M.6    Van Der Goot, F.G.7
  • 23
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • Kabsch, W. (2010) Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 26
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J. P., and Leslie, A. G. (1996) Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D Biol. Crystallogr. 52, 30-42
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.2
  • 27
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan, K. D., and Zhang, K. Y. (1999) Density modification for macromolecular phase improvement. Prog. Biophys. Mol. Biol. 72, 245-270
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 28
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M., and Paciorek, W. (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D Biol. Crystallogr. 59, 2023-2030
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 34
    • 33144462070 scopus 로고    scopus 로고
    • Glycerol monolaurate inhibits the effects of Gram-positive select agents on eukaryotic cells
    • Peterson, M. L., and Schlievert, P. M. (2006) Glycerol monolaurate inhibits the effects of Gram-positive select agents on eukaryotic cells. Biochemistry 45, 2387-2397
    • (2006) Biochemistry , vol.45 , pp. 2387-2397
    • Peterson, M.L.1    Schlievert, P.M.2
  • 36
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh, T. R., Gao, H., Baxter, W. T., Asturias, F. J., Boisset, N., Leith, A., and Frank, J. (2008) SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat. Protoc. 3, 1941-1974
    • (2008) Nat. Protoc. , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1    Gao, H.2    Baxter, W.T.3    Asturias, F.J.4    Boisset, N.5    Leith, A.6    Frank, J.7
  • 37
    • 77957322190 scopus 로고    scopus 로고
    • Classification of structural heterogeneity by maximum-likelihood methods
    • Scheres, S. H. (2010) Classification of structural heterogeneity by maximum-likelihood methods. Methods Enzymol. 482, 295-320
    • (2010) Methods Enzymol. , vol.482 , pp. 295-320
    • Scheres, S.H.1
  • 39
    • 25144494651 scopus 로고    scopus 로고
    • Fourier shell correlation threshold criteria
    • van Heel, M., and Schatz, M. (2005) Fourier shell correlation threshold criteria. J. Struct. Biol. 151, 250-262
    • (2005) J. Struct. Biol. , vol.151 , pp. 250-262
    • Van Heel, M.1    Schatz, M.2
  • 40
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 41
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 42
    • 1842689787 scopus 로고    scopus 로고
    • The identification and structure of the membrane-spanning domain of the Clostridium septicum α toxin
    • Melton, J. A., Parker, M. W., Rossjohn, J., Buckley, J. T., and Tweten, R. K. (2004) The identification and structure of the membrane-spanning domain of the Clostridium septicum α toxin. J. Biol. Chem. 279, 14315-14322
    • (2004) J. Biol. Chem. , vol.279 , pp. 14315-14322
    • Melton, J.A.1    Parker, M.W.2    Rossjohn, J.3    Buckley, J.T.4    Tweten, R.K.5
  • 43
    • 3542993232 scopus 로고    scopus 로고
    • Clostridium perfringens ε-toxin shows structural similarity to the pore-forming toxin aerolysin
    • Cole, A. R., Gibert, M., Popoff, M., Moss, D. S., Titball, R. W., and Basak, A. K. (2004) Clostridium perfringens ε-toxin shows structural similarity to the pore-forming toxin aerolysin. Nat. Struct. Mol. Biol. 11, 797-798
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 797-798
    • Cole, A.R.1    Gibert, M.2    Popoff, M.3    Moss, D.S.4    Titball, R.W.5    Basak, A.K.6
  • 44
    • 0027976196 scopus 로고
    • Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
    • Parker, M. W., Buckley, J. T., Postma, J. P., Tucker, A. D., Leonard, K., Pattus, F., and Tsernoglou, D. (1994) Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature 367, 292-295
    • (1994) Nature , vol.367 , pp. 292-295
    • Parker, M.W.1    Buckley, J.T.2    Postma, J.P.3    Tucker, A.D.4    Leonard, K.5    Pattus, F.6    Tsernoglou, D.7
  • 45
    • 20444471526 scopus 로고    scopus 로고
    • Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars
    • Mancheño, J. M., Tateno, H., Goldstein, I. J., Martínez-Ripoll, M., and Hermoso, J. A. (2005) Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars. J. Biol. Chem. 280, 17251-17259
    • (2005) J. Biol. Chem. , vol.280 , pp. 17251-17259
    • Mancheño, J.M.1    Tateno, H.2    Goldstein, I.J.3    Martínez-Ripoll, M.4    Hermoso, J.A.5
  • 48
    • 0021645447 scopus 로고
    • Multivariate statistical classification of noisy images (randomly oriented biological macromolecules)
    • van Heel, M. (1984) Multivariate statistical classification of noisy images (randomly oriented biological macromolecules). Ultramicroscopy 13, 165-183
    • (1984) Ultramicroscopy , vol.13 , pp. 165-183
    • Van Heel, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.