메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Structural basis for self-assembly of a cytolytic pore lined by protein and lipid

Author keywords

[No Author keywords available]

Indexed keywords

FRAGACEATOXIN C; LIPID; PORE FORMING CYTOTOXIC PROTEIN; PROTEIN; SEA ANEMONE TOXIN; UNCLASSIFIED DRUG; COELENTERATE VENOM; HEMOLYTIC AGENT;

EID: 84923873558     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7337     Document Type: Article
Times cited : (183)

References (54)
  • 1
    • 52949087550 scopus 로고    scopus 로고
    • Disparate proteins use similar architectures to damage membranes
    • Anderluh, G. & Lakey, J. H. Disparate proteins use similar architectures to damage membranes. Trends Biochem. Sci. 33, 482-490 (2008).
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 482-490
    • Anderluh, G.1    Lakey, J.H.2
  • 2
    • 34548666167 scopus 로고    scopus 로고
    • A common fold mediates vertebrate defense and bacterial attack
    • Rosado, C. J. et al. A common fold mediates vertebrate defense and bacterial attack. Science 317, 1548-1551 (2007).
    • (2007) Science , vol.317 , pp. 1548-1551
    • Rosado, C.J.1
  • 3
    • 84862605391 scopus 로고    scopus 로고
    • Packing a punch: The mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins
    • Dunstone, M. A. & Tweten, R. K. Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins. Curr. Opin. Struct. Biol. 22, 342-349 (2012).
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 5
    • 33750684655 scopus 로고    scopus 로고
    • Bacterial protein toxins and lipids: Pore formation or toxin entry into cells
    • Geny, B. & Popoff, M. R. Bacterial protein toxins and lipids: pore formation or toxin entry into cells. Biol. Cell 98, 667-678 (2006).
    • (2006) Biol. Cell , vol.98 , pp. 667-678
    • Geny, B.1    Popoff, M.R.2
  • 7
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism
    • Mueller, M., Grauschopf, U., Maier, T., Glockshuber, R. & Ban, N. The structure of a cytolytic alpha-helical toxin pore reveals its assembly mechanism. Nature 459, 726-730 (2009).
    • (2009) Nature , vol.459 , pp. 726-730
    • Mueller, M.1    Grauschopf, U.2    Maier, T.3    Glockshuber, R.4    Ban, N.5
  • 8
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-haemolysin, a heptameric transmembrane pore
    • Song, L. et al. Structure of staphylococcal alpha-haemolysin, a heptameric transmembrane pore. Science 274, 1859-1866 (1996).
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1
  • 9
    • 80054794259 scopus 로고    scopus 로고
    • Crystal structure of the octameric pore of staphylococcal gamma-haemolysin reveals the beta-barrel pore formation mechanism by two components
    • Yamashita, K. et al. Crystal structure of the octameric pore of staphylococcal gamma-haemolysin reveals the beta-barrel pore formation mechanism by two components. Proc. Natl Acad. Sci. USA 108, 17314-17319 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 17314-17319
    • Yamashita, K.1
  • 10
    • 79956294243 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins
    • De, S. & Olson, R. Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins. Proc. Natl Acad. Sci. USA 108, 7385-7390 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 7385-7390
    • De, S.1    Olson, R.2
  • 11
    • 68949150783 scopus 로고    scopus 로고
    • Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea
    • Bellomio, A. et al. Purification, cloning and characterization of fragaceatoxin C, a novel actinoporin from the sea anemone Actinia fragacea. Toxicon 54, 869-880 (2009).
    • (2009) Toxicon , vol.54 , pp. 869-880
    • Bellomio, A.1
  • 12
    • 79959972141 scopus 로고    scopus 로고
    • The behavior of sea anemone actinoporins at the water-membrane interface
    • Garcia-Ortega, L. et al. The behavior of sea anemone actinoporins at the water-membrane interface. Biochim. Biophys. Acta 1808, 2275-2288 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2275-2288
    • Garcia-Ortega, L.1
  • 13
    • 0023895943 scopus 로고
    • Isolation and characterization of three lethal and hemolytic toxins from the sea-anemone Actinia-Equinia L
    • Macek, P. & Lebez, D. Isolation and characterization of three lethal and hemolytic toxins from the sea-anemone Actinia-Equinia L. Toxicon 26, 441-451 (1988).
    • (1988) Toxicon , vol.26 , pp. 441-451
    • MacEk, P.1    Lebez, D.2
  • 14
    • 49649095215 scopus 로고    scopus 로고
    • Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin
    • Bakrac, B. et al. Molecular determinants of sphingomyelin specificity of a eukaryotic pore-forming toxin. J. Biol. Chem. 283, 18665-18677 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 18665-18677
    • Bakrac, B.1
  • 15
    • 4544345157 scopus 로고    scopus 로고
    • Lipid phase coexistence favors membrane insertion of equinatoxin-II, a pore-forming toxin from Actinia equina
    • Barlic, A. et al. Lipid phase coexistence favors membrane insertion of equinatoxin-II, a pore-forming toxin from Actinia equina. J. Biol. Chem. 279, 34209-34216 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 34209-34216
    • Barlic, A.1
  • 16
    • 47749109057 scopus 로고    scopus 로고
    • Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence
    • Schon, P. et al. Equinatoxin II permeabilizing activity depends on the presence of sphingomyelin and lipid phase coexistence. Biophys. J. 95, 691-698 (2008).
    • (2008) Biophys. J. , vol.95 , pp. 691-698
    • Schon, P.1
  • 17
    • 79551691895 scopus 로고    scopus 로고
    • Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
    • Mechaly, A. E. et al. Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins. Structure 19, 181-191 (2011).
    • (2011) Structure , vol.19 , pp. 181-191
    • Mechaly, A.E.1
  • 18
    • 0242542032 scopus 로고    scopus 로고
    • Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation
    • Mancheno, J. M., Martin-Benito, J., Martinez-Ripoll, M., Gavilanes, J. G. & Hermoso, J. A. Crystal and electron microscopy structures of sticholysin II actinoporin reveal insights into the mechanism of membrane pore formation. Structure 11, 1319-1328 (2003).
    • (2003) Structure , vol.11 , pp. 1319-1328
    • Mancheno, J.M.1    Martin-Benito, J.2    Martinez-Ripoll, M.3    Gavilanes, J.G.4    Hermoso, J.A.5
  • 19
    • 46049090171 scopus 로고    scopus 로고
    • A lipidic-sponge phase screen for membrane protein crystallization
    • Wohri, A. B. et al. A lipidic-sponge phase screen for membrane protein crystallization. Structure 16, 1003-1009 (2008).
    • (2008) Structure , vol.16 , pp. 1003-1009
    • Wohri, A.B.1
  • 20
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg, D., Schwarz, E., Komaromy, M. & Wall, R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125-142 (1984).
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 21
    • 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. & Gouaux, E. Crystal structure of Staphylococcal LukF delineates conformational changes accompanying formation of a transmembrane channel. Nat. Struct. Biol. 6, 134-140 (1999).
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 134-140
    • Olson, R.1    Nariya, H.2    Yokota, K.3    Kamio, Y.4    Gouaux, E.5
  • 22
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 84875154530 scopus 로고    scopus 로고
    • 2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes
    • Maula, T. et al. 2NH and 3OH are crucial structural requirements in sphingomyelin for sticholysin II binding and pore formation in bilayer membranes. Biochim. Biophys. Acta 1828, 1390-1395 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1390-1395
    • Maula, T.1
  • 24
    • 0035115356 scopus 로고    scopus 로고
    • Differential interaction of equinatoxin II with model membranes in response to lipid composition
    • Caaveiro, J. M. M. et al. Differential interaction of equinatoxin II with model membranes in response to lipid composition. Biophys. J. 80, 1343-1353 (2001).
    • (2001) Biophys. J. , vol.80 , pp. 1343-1353
    • Caaveiro, J.M.M.1
  • 26
    • 84879123070 scopus 로고    scopus 로고
    • Disulfide-bond scanning reveals assembly state and beta-strand tilt angle of the PFO beta-barrel
    • Sato, T. K., Tweten, R. K. & Johnson, A. E. Disulfide-bond scanning reveals assembly state and beta-strand tilt angle of the PFO beta-barrel. Nat. Chem. Biol. 9, 383-389 (2013).
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 383-389
    • Sato, T.K.1    Tweten, R.K.2    Johnson, A.E.3
  • 27
    • 84884511250 scopus 로고    scopus 로고
    • Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism
    • Degiacomi, M. T. et al. Molecular assembly of the aerolysin pore reveals a swirling membrane-insertion mechanism. Nat. Chem. Biol. 9, 623-629 (2013).
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 623-629
    • Degiacomi, M.T.1
  • 28
    • 0036829075 scopus 로고    scopus 로고
    • Two-step membrane binding by equinatoxin II, a pore-forming toxin from the sea anemone, involves an exposed aromatic cluster and a flexible helix
    • Hong, Q. et al. Two-step membrane binding by equinatoxin II, a pore-forming toxin from the sea anemone, involves an exposed aromatic cluster and a flexible helix. J. Biol. Chem. 277, 41916-41924 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 41916-41924
    • Hong, Q.1
  • 29
    • 8744244482 scopus 로고    scopus 로고
    • Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich
    • Kristan, K. et al. Pore formation by equinatoxin, a eukaryotic pore-forming toxin, requires a flexible N-terminal region and a stable beta-sandwich. J. Biol. Chem. 279, 46509-46517 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 46509-46517
    • Kristan, K.1
  • 30
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee, A. G. Lipid-protein interactions in biological membranes: a structural perspective. Biochim. Biophys. Acta 1612, 1-40 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 31
    • 82955206472 scopus 로고    scopus 로고
    • Rapid assembly of a multimeric membrane protein pore
    • Thompson, J. R., Cronin, B., Bayley, H. & Wallace, M. I. Rapid assembly of a multimeric membrane protein pore. Biophys. J. 101, 2679-2683 (2011).
    • (2011) Biophys. J. , vol.101 , pp. 2679-2683
    • Thompson, J.R.1    Cronin, B.2    Bayley, H.3    Wallace, M.I.4
  • 32
    • 84867906864 scopus 로고    scopus 로고
    • Pores of the toxin FraC assemble into 2D hexagonal clusters in both crystal structures and model membranes
    • Mechaly, A. E. et al. Pores of the toxin FraC assemble into 2D hexagonal clusters in both crystal structures and model membranes. J. Struct. Biol. 180, 312-317 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 312-317
    • Mechaly, A.E.1
  • 33
    • 33745748447 scopus 로고    scopus 로고
    • Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state
    • Eifler, N. et al. Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state. EMBO J. 25, 2652-2661 (2006).
    • (2006) EMBO J. , vol.25 , pp. 2652-2661
    • Eifler, N.1
  • 34
    • 69349098830 scopus 로고    scopus 로고
    • The protective antigen component of anthrax toxin forms functional octameric complexes
    • Kintzer, A. F. et al. The protective antigen component of anthrax toxin forms functional octameric complexes. J. Mol. Biol. 392, 614-629 (2009).
    • (2009) J. Mol. Biol. , vol.392 , pp. 614-629
    • Kintzer, A.F.1
  • 35
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • Tilley, S. J., Orlova, E. V., Gilbert, R. J. C., Andrew, P. W. & Saibil, H. R. Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121, 247-256 (2005).
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Gilbert, R.J.C.3    Andrew, P.W.4    Saibil, H.R.5
  • 37
    • 84863981448 scopus 로고    scopus 로고
    • Viroporins: Structure and biological functions
    • Nieva, J. L., Madan, V. & Carrasco, L. Viroporins: structure and biological functions. Nat. Rev. Microbiol. 10, 563-574 (2012).
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 563-574
    • Nieva, J.L.1    Madan, V.2    Carrasco, L.3
  • 38
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • Kawate, T., Michel, J. C., Birdsong, W. T. & Gouaux, E. Crystal structure of the ATP-gated P2X(4) ion channel in the closed state. Nature 460, 592-598 (2009).
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 39
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J., Scheuer, T., Zheng, N. & Catterall, W. A. The crystal structure of a voltage-gated sodium channel. Nature 475, 353-358 (2011).
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 40
    • 84865984564 scopus 로고    scopus 로고
    • Sea anemone (cnidaria, anthozoa, actiniaria) toxins: An overview
    • Frazao, B., Vasconcelos, V. & Antunes, A. Sea anemone (cnidaria, anthozoa, actiniaria) toxins: an overview. Mar. Drugs 10, 1812-1851 (2012).
    • (2012) Mar. Drugs , vol.10 , pp. 1812-1851
    • Frazao, B.1    Vasconcelos, V.2    Antunes, A.3
  • 41
    • 0035004910 scopus 로고    scopus 로고
    • Effects of lipid composition on membrane permeabilization by sticholysin i and II, two cytolysins of the sea anemone Stichodactyla helianthus
    • Valcarcel, C. A. et al. Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus. Biophys. J. 80, 2761-2774 (2001).
    • (2001) Biophys. J. , vol.80 , pp. 2761-2774
    • Valcarcel, C.A.1
  • 42
    • 0242664967 scopus 로고    scopus 로고
    • Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures
    • Anderluh, G. et al. Pore formation by equinatoxin II, a eukaryotic protein toxin, occurs by induction of nonlamellar lipid structures. J. Biol. Chem. 278, 45216-45223 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 45216-45223
    • Anderluh, G.1
  • 43
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R. Phosphorus assay in column chromatography. J. Biol. Chem. 234, 466-468 (1959).
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 44
    • 33947537616 scopus 로고    scopus 로고
    • An automated microseed matrix-screening method for protein crystallization
    • D'Arcy, A., Villard, F. & Marsh, M. An automated microseed matrix-screening method for protein crystallization. Acta Crystallogr. D Biol. Crystallogr. 63, 550-554 (2007).
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 550-554
    • D'Arcy, A.1    Villard, F.2    Marsh, M.3
  • 45
    • 79961160940 scopus 로고    scopus 로고
    • Random microseeding: A theoretical and practical exploration of seed stability and seeding techniques for successful protein crystallization
    • Stewart, P. D. S., Kolek, S. A., Briggs, R. A., Chayen, N. E. & Baldock, P. F. M. Random microseeding: a theoretical and practical exploration of seed stability and seeding techniques for successful protein crystallization. Cryst. Growth Des. 11, 3432-3441 (2011).
    • (2011) Cryst. Growth Des. , vol.11 , pp. 3432-3441
    • Stewart, P.D.S.1    Kolek, S.A.2    Briggs, R.A.3    Chayen, N.E.4    Baldock, P.F.M.5
  • 46
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 49
    • 0000243829 scopus 로고
    • PROCHECK-A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK-a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 50
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H. M. et al. The protein data bank. Nucleic Acids Res. 28, 235-242 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 51
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for highthroughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W. & van Aalten, D. M. F. PRODRG: a tool for highthroughput crystallography of protein-ligand complexes. Acta Crystallogr. D 60, 1355-1363 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.F.2
  • 52
    • 0021890825 scopus 로고
    • H+-and Ca2+-induced fusion and destabilization of liposomes
    • Ellens, H., Bentz, J. & Szoka, F. C. H+-and Ca2+-induced fusion and destabilization of liposomes. Biochemistry 24, 3099-3106 (1985).
    • (1985) Biochemistry , vol.24 , pp. 3099-3106
    • Ellens, H.1    Bentz, J.2    Szoka, F.C.3
  • 54
    • 63149188087 scopus 로고    scopus 로고
    • Production and biophysical characterization of the CorA transporter from Methanosarcina mazei
    • Veesler, D. et al. Production and biophysical characterization of the CorA transporter from Methanosarcina mazei. Anal. Biochem. 388, 115-121 (2009).
    • (2009) Anal. Biochem. , vol.388 , pp. 115-121
    • Veesler, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.