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Volumn 75, Issue 1, 2009, Pages 118-126

Structural characterization of the α-hemolysin monomer from Staphylococcus aureus

Author keywords

hemolysin; A toxin; Leukocidin; Molecular dynamics; Molecular modeling; SAXS (small angle X ray scattering)

Indexed keywords

ALPHA HEMOLYSIN; MONOMER;

EID: 65249138977     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22227     Document Type: Article
Times cited : (19)

References (48)
  • 2
    • 0031454754 scopus 로고    scopus 로고
    • α-Hemolysin, γ-hemolysin, and leukocidin from Staphylococcus aureus: Distant in sequence but similar in structure
    • Gouaux E, Hobaugh M, Song L. α-Hemolysin, γ-hemolysin, and leukocidin from Staphylococcus aureus: distant in sequence but similar in structure. Protein Sci 1997;6:2631-2635.
    • (1997) Protein Sci , vol.6 , pp. 2631-2635
    • Gouaux, E.1    Hobaugh, M.2    Song, L.3
  • 3
    • 0030735356 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages
    • Valeva A, Palmer M, Bhakdi S. Staphylococcal alpha-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry 1997;36:13298-13304.
    • (1997) Biochemistry , vol.36 , pp. 13298-13304
    • Valeva, A.1    Palmer, M.2    Bhakdi, S.3
  • 4
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmem-brane pore
    • Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE. Structure of staphylococcal α-hemolysin, a heptameric transmem-brane pore. Science 1996;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
  • 5
    • 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 1999;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
  • 6
    • 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
    • Pedelacq JD, Maveyraud L, Prevost G, Baba-Moussa L, Gonzalez A, Courcelle E, Shepard W, Monteil H, Samama JP, Mourey L. 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. Structure 1999;7:277-287.
    • (1999) Structure , vol.7 , pp. 277-287
    • Pedelacq, J.D.1    Maveyraud, L.2    Prevost, G.3    Baba-Moussa, L.4    Gonzalez, A.5    Courcelle, E.6    Shepard, W.7    Monteil, H.8    Samama, J.P.9    Mourey, L.10
  • 7
    • 4644355909 scopus 로고    scopus 로고
    • Crystal structure of leucotoxin S component: New insight into the staphylococcal beta-barrel pore-forming toxins
    • Guillet V, Roblin P, Werner S, Coraiola M, Menestrina G, Monteil H, Prevost G, Mourey L. Crystal structure of leucotoxin S component: new insight into the staphylococcal beta-barrel pore-forming toxins. J Biol Chem 2004;279:41028-41037.
    • (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    Prevost, G.7    Mourey, L.8
  • 8
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux JE, Braha O, Hobaugh MR, Song L, Cheley S, Shustak C, Bayley H. Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc Natl Acad Sci USA 1994;91:12828-12831.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 9
    • 0028020468 scopus 로고
    • Triggers and switches in a self-assembling pore-forming protein
    • Bayley H. Triggers and switches in a self-assembling pore-forming protein. J Cell Biochem 1994;56:177-182.
    • (1994) J Cell Biochem , vol.56 , pp. 177-182
    • Bayley, H.1
  • 10
    • 0029240394 scopus 로고
    • An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch
    • Walker B, Braha O, Cheley S, Bayley H. An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch. Chem Biol 1995;2:99-105.
    • (1995) Chem Biol , vol.2 , pp. 99-105
    • Walker, B.1    Braha, O.2    Cheley, S.3    Bayley, H.4
  • 11
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis
    • Walker B, Krishnasastry M, Zorn L, Bayley H. Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis. J Biol Chem 1992;267:21782-21786.
    • (1992) J Biol Chem , vol.267 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 12
    • 0025787798 scopus 로고
    • α-toxin of Staphylococcus aureus
    • Bhakdi S, Tranum-Jensen J. α-toxin of Staphylococcus aureus. Microbiol Rev 1991;55:733-751.
    • (1991) Microbiol Rev , vol.55 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 13
    • 33746590221 scopus 로고    scopus 로고
    • Transport of α-helical peptides through α-hemolysin and aerolysin pores
    • Stefureac R, Long Y-T, Kraatz H-B, Howard P, Lee JS. Transport of α-helical peptides through α-hemolysin and aerolysin pores. Biochemistry 2006;45:9172-9179.
    • (2006) Biochemistry , vol.45 , pp. 9172-9179
    • Stefureac, R.1    Long, Y.-T.2    Kraatz, H.-B.3    Howard, P.4    Lee, J.S.5
  • 14
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • Tilley SJ, Saibil HR. The mechanism of pore formation by bacterial toxins. Curr Opin Struct Biol 2006;16:230-236.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 15
    • 0035805604 scopus 로고    scopus 로고
    • Membrane insertion of the heptameric staphylococcal α-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane
    • Valeva A, Schnabel R, Walev I, Boukhallouk F, Bhakdi S, Palmer M. Membrane insertion of the heptameric staphylococcal α-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane. J Biol Chem 2001;276:14835-14841.
    • (2001) J Biol Chem , vol.276 , pp. 14835-14841
    • Valeva, A.1    Schnabel, R.2    Walev, I.3    Boukhallouk, F.4    Bhakdi, S.5    Palmer, M.6
  • 16
    • 0027316337 scopus 로고
    • Staphylococcus aureus α-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cyste-ine at positions 69, 130, and 186
    • Palmer M, Jursch R, Weller U, Valeva A, Hilgert K, Kehoe M, Bhakdi S. Staphylococcus aureus α-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cyste-ine at positions 69, 130, and 186. J Biol Chem 1993;268:11959-11962.
    • (1993) J Biol Chem , vol.268 , pp. 11959-11962
    • Palmer, M.1    Jursch, R.2    Weller, U.3    Valeva, A.4    Hilgert, K.5    Kehoe, M.6    Bhakdi, S.7
  • 17
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: The European molecular biology Open software suite
    • Rice P, Longden I, Bleasby A. EMBOSS: the European molecular biology Open software suite. Trends Genet 2000;16:276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 18
    • 65249096895 scopus 로고    scopus 로고
    • Parrish W, Langford JI. Powder and related techniques: X-ray techniques. In: Prince E, editor. International tables for crystallography; mathematical, physical and chemical tables. 3rd ed. C. Dordrecht, Boston, London: Kluwer Academic Publishers; 2004. pp 71-79.
    • Parrish W, Langford JI. Powder and related techniques: X-ray techniques. In: Prince E, editor. International tables for crystallography; mathematical, physical and chemical tables. 3rd ed. Volume C. Dordrecht, Boston, London: Kluwer Academic Publishers; 2004. pp 71-79.
  • 19
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 1992;25:495-503.
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.1
  • 20
    • 0000897622 scopus 로고
    • A new method for the evaluation of small-angle scattering data
    • Glatter O. A new method for the evaluation of small-angle scattering data. J Appl Crystallogr 1977;10:415-421.
    • (1977) J Appl Crystallogr , vol.10 , pp. 415-421
    • Glatter, O.1
  • 21
    • 34247493236 scopus 로고    scopus 로고
    • Matplotlib: A 2D graphics environment
    • Hunter JD. Matplotlib: a 2D graphics environment. Comput Sci Eng 2007;9:90-99.
    • (2007) Comput Sci Eng , vol.9 , pp. 90-99
    • Hunter, J.D.1
  • 22
    • 0029185933 scopus 로고
    • CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C, Koch MHJ. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 1995;28:768-773.
    • (1995) J Appl Crystallogr , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 23
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993;234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 24
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A, Do RK, Sali A. Modeling of loops in protein structures. Protein Sci 2000;9:1753-1773.
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 25
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen M-Y, Sali A. Statistical potential for assessment and prediction of protein structures. Protein Sci 2006;15:2507-2524.
    • (2006) Protein Sci , vol.15 , pp. 2507-2524
    • Shen, M.-Y.1    Sali, A.2
  • 26
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: Force-field parameterization in crystal space
    • Krieger E, Darden T, Nabuurs SB, Finkelstein A, Vriend G. Making optimal use of empirical energy functions: force-field parameterization in crystal space. Proteins 2004;57:678-683.
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 27
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA - a self-parameterizing force field
    • Krieger E, Koraimann G, Vriend G. Increasing the precision of comparative models with YASARA NOVA - a self-parameterizing force field. Proteins 2002;47:393-402.
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 30
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider TD, Stephens RM. Sequence logos: a new way to display consensus sequences. Nucleic Acids Res 1990;18:6097-6100.
    • (1990) Nucleic Acids Res , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 33
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macro-molecules from solution scattering using simulated annealing
    • Svergun DI. Restoring low resolution structure of biological macro-molecules from solution scattering using simulated annealing. Biophys J 1999;76:2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 34
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI. Uniqueness of ab initio shape determination in small-angle scattering. J Appl Crystallogr 2003;36:860-864.
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 35
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin MB, Svergun DI. Automated matching of high- and low-resolution structural models. J Appl Crystallogr 2001;34:33-41.
    • (2001) J Appl Crystallogr , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 36
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner MF, Olson AJ, Spehner JC. Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 1996;38:305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3
  • 37
    • 2442650172 scopus 로고    scopus 로고
    • High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: Implication for understanding protein-lipid interactions
    • Galdiero S, Gouaux E. High resolution crystallographic studies of alpha-hemolysin-phospholipid complexes define heptamer-lipid head group interactions: implication for understanding protein-lipid interactions. Protein Sci 2004;13:1503-1511.
    • (2004) Protein Sci , vol.13 , pp. 1503-1511
    • Galdiero, S.1    Gouaux, E.2
  • 38
    • 33846886308 scopus 로고    scopus 로고
    • Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a)
    • Dimasi N, Roessle M, Moran O, Candiano G, Svergun DI, Biassoni R. Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a). Int J Biol Macromol 2007;40:193-200.
    • (2007) Int J Biol Macromol , vol.40 , pp. 193-200
    • Dimasi, N.1    Roessle, M.2    Moran, O.3    Candiano, G.4    Svergun, D.I.5    Biassoni, R.6
  • 39
    • 0035834540 scopus 로고    scopus 로고
    • Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 Å resolution
    • Trapani S, Linss J, Goldenberg S, Fischer H, Craievich AF, Oliva G. Crystal structure of the dimeric phosphoenolpyruvate carboxykinase (PEPCK) from Trypanosoma cruzi at 2 Å resolution. J Mol Biol 2001;313:1059-1072.
    • (2001) J Mol Biol , vol.313 , pp. 1059-1072
    • Trapani, S.1    Linss, J.2    Goldenberg, S.3    Fischer, H.4    Craievich, A.F.5    Oliva, G.6
  • 40
    • 0035937246 scopus 로고    scopus 로고
    • Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR
    • Egea PF, Rochel N, Birck C, Vachette P, Timmins PA, Moras D. Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR. J Mol Biol 2001;307:557-576.
    • (2001) J Mol Biol , vol.307 , pp. 557-576
    • Egea, P.F.1    Rochel, N.2    Birck, C.3    Vachette, P.4    Timmins, P.A.5    Moras, D.6
  • 41
    • 38049186986 scopus 로고    scopus 로고
    • The structure of a full-length response regulator from ycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state
    • King-Scott J, Nowak E, Mylonas E, Panjikar S, Roessle M, Svergun DI, Tucker PA. The structure of a full-length response regulator from ycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state. J Biol Chem 2007;282:37717-37729.
    • (2007) J Biol Chem , vol.282 , pp. 37717-37729
    • King-Scott, J.1    Nowak, E.2    Mylonas, E.3    Panjikar, S.4    Roessle, M.5    Svergun, D.I.6    Tucker, P.A.7
  • 43
    • 0036128759 scopus 로고    scopus 로고
    • Subunit composition of a bicomponent toxin: Staphylococcal leukocidin forms an octameric trans-membrane pore
    • Miles G, Movileanu L, Bayley H. Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric trans-membrane pore. Protein Sci 2002;11:894-902.
    • (2002) Protein Sci , vol.11 , pp. 894-902
    • Miles, G.1    Movileanu, L.2    Bayley, H.3
  • 44
    • 25844526536 scopus 로고    scopus 로고
    • The leukocidin pore: Evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis
    • Jayasinghe L, Bayley H. The leukocidin pore: evidence for an octamer with four LukF subunits and four LukS subunits alternating around a central axis. Protein Sci 2005;14:2550-2561.
    • (2005) Protein Sci , vol.14 , pp. 2550-2561
    • Jayasinghe, L.1    Bayley, H.2
  • 45
    • 33644859965 scopus 로고    scopus 로고
    • Role of the amino latch of staphylococcal alpha -hemolysin in pore formation: A co-operative interaction between the N terminus and position 217
    • Jayasinghe L, Miles G, Bayley H. Role of the amino latch of staphylococcal alpha -hemolysin in pore formation: a co-operative interaction between the N terminus and position 217. J Biol Chem 2006;281:2195-2204.
    • (2006) J Biol Chem , vol.281 , pp. 2195-2204
    • Jayasinghe, L.1    Miles, G.2    Bayley, H.3
  • 46
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier J, Osguthorpe DJ, Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol 1978;120:97-120.
    • (1978) J Mol Biol , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 47
    • 0023237149 scopus 로고
    • Membrane-damaging action of staphylococcal α-toxin on phospholipid-cholesterol liposomes
    • Watanabe M, Tomita T, Yasuda T. Membrane-damaging action of staphylococcal α-toxin on phospholipid-cholesterol liposomes. Biochim Biophys Acta 1987;898:257-265.
    • (1987) Biochim Biophys Acta , vol.898 , pp. 257-265
    • Watanabe, M.1    Tomita, T.2    Yasuda, T.3


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