메뉴 건너뛰기




Volumn 95, Issue 5, 2008, Pages 2265-2274

Model-based prediction of the α-hemolysin structure in the hexameric state

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN; DIMYRISTOYLPHOSPHATIDYLCHOLINE; HEMOLYSIN; ION CHANNEL; STAPHYLOCOCCAL ALPHA-TOXIN; STAPHYLOCOCCUS ALPHA TOXIN;

EID: 51649089665     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.127019     Document Type: Article
Times cited : (22)

References (47)
  • 1
    • 0025787798 scopus 로고
    • α-toxin of Staphylococcus aureus
    • Bhakdi, S., and J. Tranum-Jensen. 1991. α-toxin of Staphylococcus aureus. Microbiol. Rev. 55:733-751.
    • (1991) Microbiol. Rev , vol.55 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 2
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore
    • Song, L., M. R. Hobaugh, C. Shustak, S. Cheley, H. Bayley, and J. E. Gouaux. 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
  • 3
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers
    • Czajkowsky, D. M., S. Sheng, and Z. Shao. 1998. Staphylococcal α-hemolysin can form hexamers in phospholipid bilayers. J. Mol. Biol. 276:325-330.
    • (1998) J. Mol. Biol , vol.276 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.2    Shao, Z.3
  • 4
    • 34247537938 scopus 로고    scopus 로고
    • A storable encapsulated bilayer chip containing a single protein nanopore
    • Kang, X. F., S. Cheley, A. C. Rice-Ficht, and H. Bayley. 2007. A storable encapsulated bilayer chip containing a single protein nanopore. J. Am. Chem. Soc. 129:4701-4705.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 4701-4705
    • Kang, X.F.1    Cheley, S.2    Rice-Ficht, A.C.3    Bayley, H.4
  • 5
    • 0014261629 scopus 로고
    • Interaction of staphylococcal α-toxin with artificial and natural membranes
    • Freer, J. H., J. P. Arbuthnott, and A. W. Bernheimer. 1968. Interaction of staphylococcal α-toxin with artificial and natural membranes. J. Bacteriol. 95:1153-1168.
    • (1968) J. Bacteriol , vol.95 , pp. 1153-1168
    • Freer, J.H.1    Arbuthnott, J.P.2    Bernheimer, A.W.3
  • 6
    • 0032508971 scopus 로고    scopus 로고
    • The interaction of Staphylococcus aureus bi-component γ-hemolysins and leucocidins with cells and lipid membranes
    • Ferreras, M., F. Hoper, M. D. Serra, D. A. Colin, G. Prevost, and G. Menestrina. 1998. The interaction of Staphylococcus aureus bi-component γ-hemolysins and leucocidins with cells and lipid membranes. Biochim. Biophys. Acta. 1414:108-126.
    • (1998) Biochim. Biophys. Acta , vol.1414 , pp. 108-126
    • Ferreras, M.1    Hoper, F.2    Serra, M.D.3    Colin, D.A.4    Prevost, G.5    Menestrina, G.6
  • 7
    • 0030735356 scopus 로고    scopus 로고
    • Staphylococcal α-toxin: Formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages
    • Valeva, A., M. Palmer, and S. Bhakdi. 1997. Staphylococcal α-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry. 36:13298-13304.
    • (1997) Biochemistry , vol.36 , pp. 13298-13304
    • Valeva, A.1    Palmer, M.2    Bhakdi, S.3
  • 8
    • 0022504362 scopus 로고
    • Ionic channel formed by Staphylococcus aureus α-toxin: Voltage dependent inhibition by divalent and trivalent cations
    • Menestrina, G. 1986. Ionic channel formed by Staphylococcus aureus α-toxin: voltage dependent inhibition by divalent and trivalent cations. J. Membr. Biol. 90:177-190.
    • (1986) J. Membr. Biol , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 10
    • 0033594410 scopus 로고    scopus 로고
    • Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter
    • Gu, L.-Q., O. Braha, S. Conlan, S. Cheley, and H. Bayley. 1999. Stochastic sensing of organic analytes by a pore-forming protein containing a molecular adapter. Nature. 398:686-690.
    • (1999) Nature , vol.398 , pp. 686-690
    • Gu, L.-Q.1    Braha, O.2    Conlan, S.3    Cheley, S.4    Bayley, H.5
  • 11
    • 0030465241 scopus 로고    scopus 로고
    • Characterization of individual polynucleotide molecules using a membrane channel
    • Kasianowicz, J. J., E. Brandin, D. Branton, and D. W. Deamer. 1996. Characterization of individual polynucleotide molecules using a membrane channel. Proc. Natl. Acad. Sci. USA. 93:13770-13773.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13770-13773
    • Kasianowicz, J.J.1    Brandin, E.2    Branton, D.3    Deamer, D.W.4
  • 12
    • 0034930381 scopus 로고    scopus 로고
    • Sequence-specific detection of individual DNA strands using engineered nanopores
    • Howorka, S., S. Cheley, and H. Bayley. 2001. Sequence-specific detection of individual DNA strands using engineered nanopores. Nat. Biotechnol. 19:636-639.
    • (2001) Nat. Biotechnol , vol.19 , pp. 636-639
    • Howorka, S.1    Cheley, S.2    Bayley, H.3
  • 13
    • 0023071990 scopus 로고
    • Pore formation by Staphylococcus aureus α-toxin in lipid bilayers. Dependence upon temperature and toxin concentration
    • Belmonte, G., L. Cescatti, B. Ferrari, T. Nicolussi, M. Ropele, and G. Menestrina. 1987. Pore formation by Staphylococcus aureus α-toxin in lipid bilayers. Dependence upon temperature and toxin concentration. Eur. Biophys. J. 14:349-358.
    • (1987) Eur. Biophys. J , vol.14 , pp. 349-358
    • Belmonte, G.1    Cescatti, L.2    Ferrari, B.3    Nicolussi, T.4    Ropele, M.5    Menestrina, G.6
  • 14
    • 0033779406 scopus 로고    scopus 로고
    • Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus α-toxin in planar lipid bilayers
    • Krasilnikov, O. V., P. G. Merzlyak, L. N. Yuldasheva, C. G. Rodrigues, S. Bhakdi, and A. Valeva. 2000. Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus α-toxin in planar lipid bilayers. Mol. Microbiol. 37:1372-1378.
    • (2000) Mol. Microbiol , vol.37 , pp. 1372-1378
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Yuldasheva, L.N.3    Rodrigues, C.G.4    Bhakdi, S.5    Valeva, A.6
  • 15
    • 0028980231 scopus 로고
    • Protonation dynamics of the α-toxin ion channel from spectral analysis of pH-dependent current fluctuations
    • Kasianowicz, J. J., and S. M. Bezrukov. 1995. Protonation dynamics of the α-toxin ion channel from spectral analysis of pH-dependent current fluctuations. Biophys. J. 69:94-105.
    • (1995) Biophys. J , vol.69 , pp. 94-105
    • Kasianowicz, J.J.1    Bezrukov, S.M.2
  • 16
    • 0242301631 scopus 로고    scopus 로고
    • Electrostatic influence on ion transport through the aHL channel
    • Misakian, M., and J. J. Kasianowicz. 2003. Electrostatic influence on ion transport through the aHL channel. J. Membr. Biol. 195:137-146.
    • (2003) J. Membr. Biol , vol.195 , pp. 137-146
    • Misakian, M.1    Kasianowicz, J.J.2
  • 19
    • 22244445788 scopus 로고    scopus 로고
    • Imaging α-hemolysin with molecular dynamics: Ionic conductance, osmotic permeability, and the electrostatic potential map
    • Aksimentiev, A., and K. Schulten. 2005. Imaging α-hemolysin with molecular dynamics: ionic conductance, osmotic permeability, and the electrostatic potential map. Biophys. J. 88:3745-3761.
    • (2005) Biophys. J , vol.88 , pp. 3745-3761
    • Aksimentiev, A.1    Schulten, K.2
  • 20
    • 15244338641 scopus 로고    scopus 로고
    • Ion permeation through the α-hemolysin channel: Theoretical studies based on Brownian dynamics and Poisson-Nernst-Plank electrodiffusion theory
    • Noskov, S. Y., W. Im, and B. Roux. 2004. Ion permeation through the α-hemolysin channel: theoretical studies based on Brownian dynamics and Poisson-Nernst-Plank electrodiffusion theory. Biophys. J. 87:2299-2309.
    • (2004) Biophys. J , vol.87 , pp. 2299-2309
    • Noskov, S.Y.1    Im, W.2    Roux, B.3
  • 21
    • 12344270062 scopus 로고    scopus 로고
    • Hybrid MD-Nernst-Planck model of the α-hemolysin conductance proprieties
    • Cozmuta, I., J. T. O'Keeffe, B. Deepak, and V. Stolc. 2005. Hybrid MD-Nernst-Planck model of the α-hemolysin conductance proprieties. Mol. Simul. 31:79-93.
    • (2005) Mol. Simul , vol.31 , pp. 79-93
    • Cozmuta, I.1    O'Keeffe, J.T.2    Deepak, B.3    Stolc, V.4
  • 22
    • 0028330220 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins. II. The observed structures
    • Murzin, A. G., A. M. Lesk, and C. Chothia. 1994. Principles determining the structure of β-sheet barrels in proteins. II. The observed structures. J. Mol. Biol. 236:1382-1400.
    • (1994) J. Mol. Biol , vol.236 , pp. 1382-1400
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 23
    • 0028348081 scopus 로고
    • Principles determining the structure of β-sheet barrels in proteins. I. A theoretical analysis
    • Murzin, A. G., A. M. Lesk, and C. Chothia. 1994. Principles determining the structure of β-sheet barrels in proteins. I. A theoretical analysis. J. Mol. Biol. 236:1369-1381.
    • (1994) J. Mol. Biol , vol.236 , pp. 1369-1381
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 25
    • 0041784950 scopus 로고    scopus 로고
    • MacKerell, A. D., D. Bashford, M. Bellott, R. L. Dunbrack, J. D. Evanseck, M. J. Field, S. Fischer, J. Gao, H. Guo, S. Ha, D. Joseph-McCarthy, L. Kuchnir, K. Kuczera, F. T. K. Lau, C. Mattos, S. Michnick, T. Ngo, D. T. Nguyen, B. Prodhom, W. E. Reiher, B. Roux, M. Schlenkrich, J. C. Smith, R. Stote, J. Straub, M. Watanabe, J. Wiorkiewicz-Kuczera, D. Yin, and M. Karplus. 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B. 102:3586-3616.
    • MacKerell, A. D., D. Bashford, M. Bellott, R. L. Dunbrack, J. D. Evanseck, M. J. Field, S. Fischer, J. Gao, H. Guo, S. Ha, D. Joseph-McCarthy, L. Kuchnir, K. Kuczera, F. T. K. Lau, C. Mattos, S. Michnick, T. Ngo, D. T. Nguyen, B. Prodhom, W. E. Reiher, B. Roux, M. Schlenkrich, J. C. Smith, R. Stote, J. Straub, M. Watanabe, J. Wiorkiewicz-Kuczera, D. Yin, and M. Karplus. 1998. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B. 102:3586-3616.
  • 28
    • 33646940952 scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23: 327-341.
    • (1977) J. Comput. Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 29
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller, S. E., Y. Zhang, R. W. Pastor, and B. R. Brooks. 1995. Constant pressure molecular dynamics simulation: the Langevin piston method. J. Chem. Phys. 103:4613-4621.
    • (1995) J. Chem. Phys , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 30
    • 0031167555 scopus 로고    scopus 로고
    • Atomic radii for continuum electrostatics calculations based on molecular dynamics free energy simulations
    • Nina, M., D. Beglov, and B. Roux. 1997. Atomic radii for continuum electrostatics calculations based on molecular dynamics free energy simulations. J. Phys. Chem. B. 101:5239-5248.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 5239-5248
    • Nina, M.1    Beglov, D.2    Roux, B.3
  • 32
    • 0016751324 scopus 로고
    • Drag coefficients for the movement of rigid spheres through liquid-filled cylindrical pores
    • Paine, P. L., and P. Scherr. 1975. Drag coefficients for the movement of rigid spheres through liquid-filled cylindrical pores. Biophys. J. 15: 1087-1091.
    • (1975) Biophys. J , vol.15 , pp. 1087-1091
    • Paine, P.L.1    Scherr, P.2
  • 33
    • 33751234250 scopus 로고    scopus 로고
    • Application of the Poisson-Nernst-Planck theory with space-dependent diffusion coefficients to KcsA
    • Furini, S., F. Zerbetto, and S. Cavalcanti. 2006. Application of the Poisson-Nernst-Planck theory with space-dependent diffusion coefficients to KcsA. Biophys. J. 91:3162-3169.
    • (2006) Biophys. J , vol.91 , pp. 3162-3169
    • Furini, S.1    Zerbetto, F.2    Cavalcanti, S.3
  • 34
    • 38149012053 scopus 로고    scopus 로고
    • Role of the intracellular cavity in potassium channel conductivity
    • Furini, S., F. Zerbetto, and S. Cavalcanti. 2007. Role of the intracellular cavity in potassium channel conductivity. J. Phys. Chem. B. 111: 13993-14000.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 13993-14000
    • Furini, S.1    Zerbetto, F.2    Cavalcanti, S.3
  • 35
    • 0030333470 scopus 로고    scopus 로고
    • Three-dimensional hydrogen-bond geometry and probability information from a crystal survey
    • Mills, J. E. J., and P. M. Dean. 1996. Three-dimensional hydrogen-bond geometry and probability information from a crystal survey. J. Comput. Aided Mol. Des. 10:607-622.
    • (1996) J. Comput. Aided Mol. Des , vol.10 , pp. 607-622
    • Mills, J.E.J.1    Dean, P.M.2
  • 37
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis
    • Walker, B., M. Krishnasastry, L. Zorn, and H. Bayley. 1992. Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis. J. Biol. Chem. 267:21782-21786.
    • (1992) J. Biol. Chem , vol.267 , pp. 21782-21786
    • Walker, B.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 38
    • 33644859965 scopus 로고    scopus 로고
    • Role of the amino latch of staphylococcal α-hemolysin in pore formation: A co-operative interaction between the N terminus and position 217
    • Jayasinghe, L., G. Miles, and H. Bayley. 2006. Role of the amino latch of staphylococcal α-hemolysin in pore formation: a co-operative interaction between the N terminus and position 217. J. Biol. Chem. 281:2195-2204.
    • (2006) J. Biol. Chem , vol.281 , pp. 2195-2204
    • Jayasinghe, L.1    Miles, G.2    Bayley, H.3
  • 40
    • 0033014096 scopus 로고    scopus 로고
    • Progress and prospects in permeation
    • Nonner, W., D. P. Chen, and B. Eisenberg. 1999. Progress and prospects in permeation. J. Gen. Physiol. 113:773-782.
    • (1999) J. Gen. Physiol , vol.113 , pp. 773-782
    • Nonner, W.1    Chen, D.P.2    Eisenberg, B.3
  • 41
    • 15244344856 scopus 로고    scopus 로고
    • Poisson-Nernst-Planck theory approach to the calculations of current through biological ion channels
    • Coalson, R. D., and M. G. Kurnikova. 2005. Poisson-Nernst-Planck theory approach to the calculations of current through biological ion channels. IEEE Trans. Nanobioscience. 4:81-93.
    • (2005) IEEE Trans. Nanobioscience , vol.4 , pp. 81-93
    • Coalson, R.D.1    Kurnikova, M.G.2
  • 42
    • 36348931530 scopus 로고    scopus 로고
    • A predictive MD-Nernst-Planck model for transport in α-hemolysin: Modeling anisotropic ion currents
    • O'Keeffe, J. T., I. Cozmuta, D. Bose, and V. Stolc. 2007. A predictive MD-Nernst-Planck model for transport in α-hemolysin: modeling anisotropic ion currents. Chem. Phys. 342:25-32.
    • (2007) Chem. Phys , vol.342 , pp. 25-32
    • O'Keeffe, J.T.1    Cozmuta, I.2    Bose, D.3    Stolc, V.4
  • 43
    • 0035169385 scopus 로고    scopus 로고
    • Prolonged residence time of a noncovalent molecular adapter, β-cyclodextrin, within the lumen of mutant α-hemolysin pores
    • Gu, L.-Q., S. Cheley, and H. Bayley. 2001. Prolonged residence time of a noncovalent molecular adapter, β-cyclodextrin, within the lumen of mutant α-hemolysin pores. J. Gen. Physiol. 118:481-494.
    • (2001) J. Gen. Physiol , vol.118 , pp. 481-494
    • Gu, L.-Q.1    Cheley, S.2    Bayley, H.3
  • 45
    • 0033776849 scopus 로고    scopus 로고
    • Detecting protein analytes that modulate transmembrane movement of a polymer chain within a single protein pore
    • Movileanu, L., S. Howorka, O. Braha, and H. Bayley. 2000. Detecting protein analytes that modulate transmembrane movement of a polymer chain within a single protein pore. Nat. Biotechnol. 18:1091-1095.
    • (2000) Nat. Biotechnol , vol.18 , pp. 1091-1095
    • Movileanu, L.1    Howorka, S.2    Braha, O.3    Bayley, H.4
  • 47
    • 0034614053 scopus 로고    scopus 로고
    • Cyclic peptides as molecular adapters for a pore-forming protein
    • Sanchez-Quesada, J., M. R. Ghadiri, H. Bayley, and O. Braha. 2000. Cyclic peptides as molecular adapters for a pore-forming protein. J. Am. Chem. Soc. 122:11757-11766.
    • (2000) J. Am. Chem. Soc , vol.122 , pp. 11757-11766
    • Sanchez-Quesada, J.1    Ghadiri, M.R.2    Bayley, H.3    Braha, O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.