메뉴 건너뛰기




Volumn 85, Issue 4, 2003, Pages 2087-2099

Gating of MscL studied by steered molecular dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BACTERIAL MEMBRANE; CALCULATION; CHANNEL GATING; CYTOPLASM; ESCHERICHIA COLI; ION CONDUCTANCE; LIPID BILAYER; MECHANOSENSITIVE CHANNEL; MEMBRANE CHANNEL; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN; SEQUENCE HOMOLOGY; SURFACE TENSION;

EID: 0141754098     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74637-2     Document Type: Article
Times cited : (144)

References (46)
  • 1
    • 0033957169 scopus 로고    scopus 로고
    • Contributions of the different extramembranous domains of the mechanosensitive ion channel MscL to its response to membrane tension
    • Ajouz, B., C. Berrier, M. Besnard, B. Martinac, and A. Ghazi. 2000. Contributions of the different extramembranous domains of the mechanosensitive ion channel MscL to its response to membrane tension. J. Biol. Chem. 275:1015-1022.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1015-1022
    • Ajouz, B.1    Berrier, C.2    Besnard, M.3    Martinac, B.4    Ghazi, A.5
  • 2
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • Bass, R. B., P. Strop, M. Barclay, and D. C. Rees. 2002. Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel. Science. 298:1582-1587.
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 3
    • 0036787715 scopus 로고    scopus 로고
    • Open-state models of a potassium channel
    • Biggin, P. C., and M. S. P. Sansom. 2002. Open-state models of a potassium channel. Biophys. J. 83:1867-1876.
    • (2002) Biophys. J. , vol.83 , pp. 1867-1876
    • Biggin, P.C.1    Sansom, M.S.P.2
  • 4
    • 0031463940 scopus 로고    scopus 로고
    • Mutations in a bacterial mechanosensitive channel change the cellular response to osmotic stress
    • Blount, P., M. J. Schroeder, and C. Kung. 1997. Mutations in a bacterial mechanosensitive channel change the cellular response to osmotic stress. J. Biol. Chem. 272:32150-32157.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32150-32157
    • Blount, P.1    Schroeder, M.J.2    Kung, C.3
  • 5
    • 0029813032 scopus 로고    scopus 로고
    • Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli
    • Blount, P., S. I. Sukharev, P. C. Moe, M. J. Schroeder, H. R. Guy, and C. Kung. 1996. Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli. EMBO J. 15:4798-4805.
    • (1996) EMBO J. , vol.15 , pp. 4798-4805
    • Blount, P.1    Sukharev, S.I.2    Moe, P.C.3    Schroeder, M.J.4    Guy, H.R.5    Kung, C.6
  • 6
    • 0004150063 scopus 로고    scopus 로고
    • Cambridge University Press, Cambridge, UK
    • Boal, D. 2002. Mechanics of the Cell. Cambridge University Press, Cambridge, UK.
    • (2002) Mechanics of the Cell
    • Boal, D.1
  • 7
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang, G., R. H. Spencer, A. T. Lee, M. T. Barclay, and D. C. Rees. 1998. Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science. 282:2220-2226.
    • (1998) Science , vol.282 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 8
    • 0020633119 scopus 로고
    • Kinetics of the receptor current in bullfrog saccular hair cells
    • Corey, D. P., and A. J. Hudspeth. 1983. Kinetics of the receptor current in bullfrog saccular hair cells. J. Neurosci. 3:962-976.
    • (1983) J. Neurosci. , vol.3 , pp. 962-976
    • Corey, D.P.1    Hudspeth, A.J.2
  • 9
    • 85031057092 scopus 로고    scopus 로고
    • Structure and conformational rearrangements of MscL N-terminal domain
    • Cortes, D. M., B. Martinac, and E. Perozo. 2003. Structure and conformational rearrangements of MscL N-terminal domain. Biophys. J. 84:21a.
    • (2003) Biophys. J. , vol.84
    • Cortes, D.M.1    Martinac, B.2    Perozo, E.3
  • 10
    • 0030866749 scopus 로고    scopus 로고
    • Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli
    • Cruickshank, C. C., R. F. Minchin, A. C. L. Dain, and B. Martinac. 1997. Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli. Biophys. J. 73:1925-1931.
    • (1997) Biophys. J. , vol.73 , pp. 1925-1931
    • Cruickshank, C.C.1    Minchin, R.F.2    Dain, A.C.L.3    Martinac, B.4
  • 11
    • 33846823909 scopus 로고
    • Particle mesh Ewald. An N·log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald. An N·log(N) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 12
    • 0034859342 scopus 로고    scopus 로고
    • Molecular dynamics simulations of wild-type and mutant forms of the Mycobacterium tuberculosis MscL channel
    • Elmore, D. E., and D. A. Dougherty. 2001. Molecular dynamics simulations of wild-type and mutant forms of the Mycobacterium tuberculosis MscL channel. Biophys. J. 81:1345-1359.
    • (2001) Biophys. J. , vol.81 , pp. 1345-1359
    • Elmore, D.E.1    Dougherty, D.A.2
  • 13
    • 0035807810 scopus 로고    scopus 로고
    • Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants
    • Fleming, K. G., and D. M. Engelman. 2001. Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants. Proc. Natl. Acad. Sci. USA. 98:14340-14344.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14340-14344
    • Fleming, K.G.1    Engelman, D.M.2
  • 15
    • 0029619259 scopus 로고
    • Knowledge-based secondary structure assignment
    • Frishman, D., and P. Argos. 1995. Knowledge-based secondary structure assignment. Prot. Struct. Func. Gen. 23:566-579.
    • (1995) Prot. Struct. Func. Gen. , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 16
    • 4243997763 scopus 로고    scopus 로고
    • Grubmüller, H. 1996. SOLVATE 1.0. http://www.mpibpc.gwdg.de/abteilungen/071/solvate/docu.html.
    • (1996) SOLVATE 1.0
    • Grubmüller, H.1
  • 19
    • 0035039272 scopus 로고    scopus 로고
    • Structural determinants of MscL gating studied by molecular dynamics simulations
    • Gullingsrud, J., D. Kosztin, and K. Schulten. 2001. Structural determinants of MscL gating studied by molecular dynamics simulations. Biophys. J. 80:2074-2081.
    • (2001) Biophys. J. , vol.80 , pp. 2074-2081
    • Gullingsrud, J.1    Kosztin, D.2    Schulten, K.3
  • 21
    • 0030834853 scopus 로고    scopus 로고
    • Binding pathway of retinal to bacteriorhodopsin: A prediction by molecular dynamics simulations
    • Isralewitz, B., S. Izrailev, and K. Schulten. 1997. Binding pathway of retinal to bacteriorhodopsin: a prediction by molecular dynamics simulations. Biophys. J. 73:2972-2979.
    • (1997) Biophys. J. , vol.73 , pp. 2972-2979
    • Isralewitz, B.1    Izrailev, S.2    Schulten, K.3
  • 24
    • 0035756772 scopus 로고    scopus 로고
    • Mechanosensitive channel of Thermoplasma, the cell wall-less Archaea: Cloning and molecular characterization
    • Kloda, A., and B. Martinac. 2001. Mechanosensitive channel of Thermoplasma, the cell wall-less Archaea: cloning and molecular characterization. Cell Biochem. Biophys. 34:321-347.
    • (2001) Cell Biochem. Biophys. , vol.34 , pp. 321-347
    • Kloda, A.1    Martinac, B.2
  • 25
    • 0037197932 scopus 로고    scopus 로고
    • Conformational pathways in the gating of Escherichia coli mechanosensitive channel
    • Kong, Y., Y. Shen, T. E. Warth, and J. Ma. 2002. Conformational pathways in the gating of Escherichia coli mechanosensitive channel. Proc. Natl. Acad. Sci. USA. 99:5999-6004.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5999-6004
    • Kong, Y.1    Shen, Y.2    Warth, T.E.3    Ma, J.4
  • 26
    • 0032906662 scopus 로고    scopus 로고
    • Unbinding of retinoic acid from its receptor studied by steered molecular dynamics
    • Kosztin, D., S. Izrailev, and K. Schulten. 1999. Unbinding of retinoic acid from its receptor studied by steered molecular dynamics. Biophys. J. 76:188-197.
    • (1999) Biophys. J. , vol.76 , pp. 188-197
    • Kosztin, D.1    Izrailev, S.2    Schulten, K.3
  • 27
    • 0034271962 scopus 로고    scopus 로고
    • Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations
    • Lindahl, E., and O. Edholm. 2000. Spatial and energetic-entropic decomposition of surface tension in lipid bilayers from molecular dynamics simulations. J. Chem. Phys. 113:3882-3893.
    • (2000) J. Chem. Phys. , vol.113 , pp. 3882-3893
    • Lindahl, E.1    Edholm, O.2
  • 28
    • 0033445338 scopus 로고    scopus 로고
    • Steered molecular dynamics simulation of conformational changes of immunoglobulin domain 127 interpret atomic force microscopy observations
    • Lu, H., and K. Schulten. 1999. Steered molecular dynamics simulation of conformational changes of immunoglobulin domain 127 interpret atomic force microscopy observations. Chem. Phys. 247:141-153.
    • (1999) Chem. Phys. , vol.247 , pp. 141-153
    • Lu, H.1    Schulten, K.2
  • 30
    • 0025114667 scopus 로고
    • Mechanosensitive ion channels of E. coli activated by amphipaths
    • Martinac, B., J. Adler, and C. Kung. 1990. Mechanosensitive ion channels of E. coli activated by amphipaths. Nature. 348:261-263.
    • (1990) Nature , vol.348 , pp. 261-263
    • Martinac, B.1    Adler, J.2    Kung, C.3
  • 31
    • 0032530833 scopus 로고    scopus 로고
    • One face of a transmembrane helix is crucial in mechanosensitive channel gating
    • Ou, X., P. Blount, R. J. Hoffman, and C. Kung. 1998. One face of a transmembrane helix is crucial in mechanosensitive channel gating. Proc. Natl. Acad. Sci. USA. 95:11471-11475.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11471-11475
    • Ou, X.1    Blount, P.2    Hoffman, R.J.3    Kung, C.4
  • 32
    • 0034884665 scopus 로고    scopus 로고
    • Site-directed spin-labeling analysis of reconstituted MscL in the closed state
    • Perozo, E., A. Kloda, D. M. Cortes, and B. Martinac. 2001. Site-directed spin-labeling analysis of reconstituted MscL in the closed state. J. Gen. Physiol. 118:193-205.
    • (2001) J. Gen. Physiol. , vol.118 , pp. 193-205
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 33
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • Perozo, E., D. M. Cortes, P. Sompornpisut, A. Kloda, and B. Martinac. 2002a. Open channel structure of MscL and the gating mechanism of mechanosensitive channels. Nature. 418:942-948.
    • (2002) Nature , vol.418 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 34
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo, E., A. Kooda, D. M. Cortes, and B. Martinac. 2002b. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat. Struct. Biol. 9:696-703.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 696-703
    • Perozo, E.1    Kooda, A.2    Cortes, D.M.3    Martinac, B.4
  • 35
    • 0036536998 scopus 로고    scopus 로고
    • Theoretical and computational models of ion channels
    • Roux, B. 2002. Theoretical and computational models of ion channels. Curr. Op. Struct. Biol. 12:182-189.
    • (2002) Curr. Op. Struct. Biol. , vol.12 , pp. 182-189
    • Roux, B.1
  • 37
    • 0027794972 scopus 로고
    • Targeted molecular dynamics simulation of conformational change application to the T↔R transition in insulin
    • Schlitter, J., M. Engels, P. Krtiger, E. Jacoby, and A. Wollmer. 1993. Targeted molecular dynamics simulation of conformational change application to the T↔R transition in insulin. Mol. Sim. 10:291-308.
    • (1993) Mol. Sim. , vol.10 , pp. 291-308
    • Schlitter, J.1    Engels, M.2    Krtiger, P.3    Jacoby, E.4    Wollmer, A.5
  • 38
    • 0027145628 scopus 로고
    • The pore dimensions of gramicidin-A
    • Smart, O., J. Goodfellow, and B. Wallace. 1993. The pore dimensions of gramicidin-A. Biophys. J. 65:2455-2460.
    • (1993) Biophys. J. , vol.65 , pp. 2455-2460
    • Smart, O.1    Goodfellow, J.2    Wallace, B.3
  • 39
    • 0035825634 scopus 로고    scopus 로고
    • The gating mechanism of the large mechanosensitive channel MscL
    • Sukharev, S., M. Betanzos, C.-S. Chiang, and H. R. Guy. 2001a. The gating mechanism of the large mechanosensitive channel MscL. Nature. 409:720-724.
    • (2001) Nature , vol.409 , pp. 720-724
    • Sukharev, S.1    Betanzos, M.2    Chiang, C.-S.3    Guy, H.R.4
  • 40
    • 0034910316 scopus 로고    scopus 로고
    • Structural models of the MscL gating mechanism
    • Sukharev, S., S. R. Durell, and H. R. Guy. 2001b. Structural models of the MscL gating mechanism. Biophys. J. 81:917-936.
    • (2001) Biophys. J. , vol.81 , pp. 917-936
    • Sukharev, S.1    Durell, S.R.2    Guy, H.R.3
  • 41
    • 0032935824 scopus 로고    scopus 로고
    • Energetics and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL
    • Sukharev, S. I., W. J. Sigurdson, C. Kung, and F. Sachs. 1999. Energetics and spatial parameters for gating of the bacterial large conductance mechanosensitive channel, MscL. J. Gen. Physiol. 113:525-539.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 525-539
    • Sukharev, S.I.1    Sigurdson, W.J.2    Kung, C.3    Sachs, F.4
  • 42
    • 0036112238 scopus 로고    scopus 로고
    • Membrane stretch accelerates activation and slow inactivation in Shaker channels with S3-S4 linker deletions
    • Tabarean, I. V., and C. E. Morris. 2002. Membrane stretch accelerates activation and slow inactivation in Shaker channels with S3-S4 linker deletions. Biophys. J. 82:2982-2994.
    • (2002) Biophys. J. , vol.82 , pp. 2982-2994
    • Tabarean, I.V.1    Morris, C.E.2
  • 44
    • 0033136019 scopus 로고    scopus 로고
    • Investigating a back door mechanism of actin phosphate release by steered molecular dynamics
    • Wriggers, W., and K. Schulten. 1999. Investigating a back door mechanism of actin phosphate release by steered molecular dynamics. Prot. Struct. Func. Gen. 35:262-273.
    • (1999) Prot. Struct. Func. Gen. , vol.35 , pp. 262-273
    • Wriggers, W.1    Schulten, K.2
  • 45
    • 8944243077 scopus 로고    scopus 로고
    • Mechanical strain induces constitutive and regulated secretion of glycosaminoglycans and proteoglycans in fetal lung cells
    • Xu, J., M. Liu, J. Liu, I. Caniggia, and M. Post. 1996. Mechanical strain induces constitutive and regulated secretion of glycosaminoglycans and proteoglycans in fetal lung cells. J. Cell Sci. 109:1605-1613.
    • (1996) J. Cell Sci. , vol.109 , pp. 1605-1613
    • Xu, J.1    Liu, M.2    Liu, J.3    Caniggia, I.4    Post, M.5
  • 46
    • 0032826458 scopus 로고    scopus 로고
    • Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity
    • Yoshimura, K., A. Batiza, M. Schroeder, P. Blount, and C. Kung. 1999. Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity. Biophys. J. 77:1960-1972.
    • (1999) Biophys. J. , vol.77 , pp. 1960-1972
    • Yoshimura, K.1    Batiza, A.2    Schroeder, M.3    Blount, P.4    Kung, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.