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Volumn 23, Issue 10, 2016, Pages 884-890

Membrane insertion of a Tc toxin in near-atomic detail

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL TOXIN; LIPID; LIPID NANODISC; MEMBRANE PROTEIN; NANODISC; TC TOXIN; TCDA1 PROTEIN; UNCLASSIFIED DRUG; MEMBRANE LIPID; PORE FORMING CYTOTOXIC PROTEIN;

EID: 84984622443     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3281     Document Type: Article
Times cited : (73)

References (57)
  • 3
    • 79953236969 scopus 로고    scopus 로고
    • Mechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process
    • Murphy, J.R. Mechanism of diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process. Toxins (Basel) 3, 294-308 (2011).
    • (2011) Toxins (Basel) , vol.3 , pp. 294-308
    • Murphy, J.R.1
  • 4
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor binding, internalization, pore formation, and translocation
    • Young, J.A.T., Collier, R.J. Anthrax toxin: receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76, 243-265 (2007).
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.T.1    Collier, R.J.2
  • 5
    • 0032568883 scopus 로고    scopus 로고
    • Insecticidal toxins from the bacterium Photorhabdus luminescens
    • Bowen, D. et al. Insecticidal toxins from the bacterium Photorhabdus luminescens. Science 280, 2129-2132 (1998).
    • (1998) Science , vol.280 , pp. 2129-2132
    • Bowen, D.1
  • 6
    • 84855505454 scopus 로고    scopus 로고
    • 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity
    • Landsberg, M.J. et al. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc. Natl. Acad. Sci. USA 108, 20544-20549 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20544-20549
    • Landsberg, M.J.1
  • 7
    • 84885632423 scopus 로고    scopus 로고
    • The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device
    • Busby, J.N., Panjikar, S., Landsberg, M.J., Hurst, M.R.H., Lott, J.S. The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device. Nature 501, 547-550 (2013).
    • (2013) Nature , vol.501 , pp. 547-550
    • Busby, J.N.1    Panjikar, S.2    Landsberg, M.J.3    Hurst, M.R.H.4    Lott, J.S.5
  • 9
    • 51249121783 scopus 로고    scopus 로고
    • How to cope with insect resistance to Bt toxins?
    • Bravo, A., Soberón, M. How to cope with insect resistance to Bt toxins? Trends Biotechnol. 26, 573-579 (2008).
    • (2008) Trends Biotechnol. , vol.26 , pp. 573-579
    • Bravo, A.1    Soberón, M.2
  • 11
    • 77649193972 scopus 로고    scopus 로고
    • Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering
    • Lang, A.E. et al. Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering. Science 327, 1139-1142 (2010).
    • (2010) Science , vol.327 , pp. 1139-1142
    • Lang, A.E.1
  • 12
    • 0028206349 scopus 로고
    • Rhs elements of Escherichia coli: A family of genetic composites each encoding a large mosaic protein
    • Hill, C.W., Sandt, C.H., Vlazny, D.A. Rhs elements of Escherichia coli: a family of genetic composites each encoding a large mosaic protein. Mol. Microbiol. 12, 865-871 (1994).
    • (1994) Mol. Microbiol. , vol.12 , pp. 865-871
    • Hill, C.W.1    Sandt, C.H.2    Vlazny, D.A.3
  • 13
    • 84897574368 scopus 로고    scopus 로고
    • Mechanism of Tc toxin action revealed in molecular detail
    • Meusch, D. et al. Mechanism of Tc toxin action revealed in molecular detail. Nature 508, 61-65 (2014).
    • (2014) Nature , vol.508 , pp. 61-65
    • Meusch, D.1
  • 14
    • 84875620662 scopus 로고    scopus 로고
    • A syringe-like injection mechanism in Photorhabdus luminescens toxins
    • Gatsogiannis, C. et al. A syringe-like injection mechanism in Photorhabdus luminescens toxins. Nature 495, 520-523 (2013).
    • (2013) Nature , vol.495 , pp. 520-523
    • Gatsogiannis, C.1
  • 15
    • 84922481432 scopus 로고    scopus 로고
    • Architecture and conformational switch mechanism of the ryanodine receptor
    • Efremov, R.G., Leitner, A., Aebersold, R., Raunser, S. Architecture and conformational switch mechanism of the ryanodine receptor. Nature 517, 39-43 (2015).
    • (2015) Nature , vol.517 , pp. 39-43
    • Efremov, R.G.1    Leitner, A.2    Aebersold, R.3    Raunser, S.4
  • 17
    • 42949161558 scopus 로고    scopus 로고
    • Binding-induced folding of a natively unstructured transcription factor
    • Turjanski, A.G., Gutkind, J.S., Best, R.B., Hummer, G. Binding-induced folding of a natively unstructured transcription factor. PLoS Comput. Biol. 4, e1000060 (2008).
    • (2008) PLoS Comput. Biol. , vol.4 , pp. e1000060
    • Turjanski, A.G.1    Gutkind, J.S.2    Best, R.B.3    Hummer, G.4
  • 18
    • 84923099296 scopus 로고    scopus 로고
    • Mechanisms of integral membrane protein insertion and folding
    • Cymer, F., von Heijne, G., White, S.H. Mechanisms of integral membrane protein insertion and folding. J. Mol. Biol. 427, 999-1022 (2015).
    • (2015) J. Mol. Biol. , vol.427 , pp. 999-1022
    • Cymer, F.1    Von Heijne, G.2    White, S.H.3
  • 19
    • 84930637225 scopus 로고    scopus 로고
    • Atomic structure of anthrax protective antigen pore elucidates toxin translocation
    • Jiang, J., Pentelute, B.L., Collier, R.J., Zhou, Z.H. Atomic structure of anthrax protective antigen pore elucidates toxin translocation. Nature 521, 545-549 (2015).
    • (2015) Nature , vol.521 , pp. 545-549
    • Jiang, J.1    Pentelute, B.L.2    Collier, R.J.3    Zhou, Z.H.4
  • 20
    • 79959545618 scopus 로고    scopus 로고
    • Charge requirements for proton gradient-driven translocation of anthrax toxin
    • Brown, M.J., Thoren, K.L., Krantz, B.A. Charge requirements for proton gradient-driven translocation of anthrax toxin. J. Biol. Chem. 286, 23189-23199 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 23189-23199
    • Brown, M.J.1    Thoren, K.L.2    Krantz, B.A.3
  • 21
    • 84860200742 scopus 로고    scopus 로고
    • Ratcheting up protein translocation with anthrax toxin
    • Feld, G.K., Brown, M.J., Krantz, B.A. Ratcheting up protein translocation with anthrax toxin. Protein Sci. 21, 606-624 (2012).
    • (2012) Protein Sci. , vol.21 , pp. 606-624
    • Feld, G.K.1    Brown, M.J.2    Krantz, B.A.3
  • 22
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • Kellermayer, M.S., Smith, S.B., Granzier, H.L., Bustamante, C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science 276, 1112-1116 (1997).
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 23
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J.M., Gaub, H.E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276, 1109-1112 (1997).
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 24
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 25
    • 84863011784 scopus 로고    scopus 로고
    • Iterative stable alignment and clustering of 2D transmission electron microscope images
    • Yang, Z., Fang, J., Chittuluru, J., Asturias, F.J., Penczek, P.A. Iterative stable alignment and clustering of 2D transmission electron microscope images. Structure 20, 237-247 (2012).
    • (2012) Structure , vol.20 , pp. 237-247
    • Yang, Z.1    Fang, J.2    Chittuluru, J.3    Asturias, F.J.4    Penczek, P.A.5
  • 26
    • 33845296470 scopus 로고    scopus 로고
    • SPARX, a new environment for Cryo-EM image processing
    • Hohn, M. et al. SPARX, a new environment for Cryo-EM image processing. J. Struct. Biol. 157, 47-55 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 47-55
    • Hohn, M.1
  • 27
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J.A., Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 28
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S.H.W. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 29
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 30
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres, S.H. Beam-induced motion correction for sub-megadalton cryo-EM particles. eLife 3, e03665 (2014).
    • (2014) ELife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 31
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F.J., Tagare, H.D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63-65 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 32
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera: A visualization system for exploratory research and analysis
    • Pettersen, E.F. et al. UCSF Chimera: a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 33
    • 84887256582 scopus 로고    scopus 로고
    • IMODFIT: Efficient and robust flexible fitting based on vibrational analysis in internal coordinates
    • Lopéz-Blanco, J.R., Chacón, P. iMODFIT: efficient and robust flexible fitting based on vibrational analysis in internal coordinates. J. Struct. Biol. 184, 261-270 (2013).
    • (2013) J. Struct. Biol. , vol.184 , pp. 261-270
    • Lopéz-Blanco, J.R.1    Chacón, P.2
  • 34
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 36
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown, A. et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D Biol. Crystallogr. 71, 136-153 (2015).
    • (2015) Acta Crystallogr. D Biol. Crystallogr. , vol.71 , pp. 136-153
    • Brown, A.1
  • 38
    • 84900435661 scopus 로고    scopus 로고
    • Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome
    • Fernández, I.S., Bai, X.-C., Murshudov, G., Scheres, S.H.W., Ramakrishnan, V. Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell 157, 823-831 (2014).
    • (2014) Cell , vol.157 , pp. 823-831
    • Fernández, I.S.1    Bai, X.-C.2    Murshudov, G.3    Scheres, S.H.W.4    Ramakrishnan, V.5
  • 39
    • 4043052866 scopus 로고    scopus 로고
    • Accurate prediction of solvent accessibility using neural networks-based regression
    • Adamczak, R., Porollo, A., Meller, J. Accurate prediction of solvent accessibility using neural networks-based regression. Proteins 56, 753-767 (2004).
    • (2004) Proteins , vol.56 , pp. 753-767
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 40
    • 84928561542 scopus 로고    scopus 로고
    • CHEXVIS: A tool for molecular channel extraction and visualization
    • Masood, T.B., Sandhya, S., Chandra, N., Natarajan, V. CHEXVIS: a tool for molecular channel extraction and visualization. BMC Bioinformatics 16, 119 (2015).
    • (2015) BMC Bioinformatics , vol.16 , pp. 119
    • Masood, T.B.1    Sandhya, S.2    Chandra, N.3    Natarajan, V.4
  • 41
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V.B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D Biol. Crystallogr. 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 42
    • 79957811210 scopus 로고    scopus 로고
    • CMView: Interactive contact map visualization and analysis
    • Vehlow, C. et al. CMView: interactive contact map visualization and analysis. Bioinformatics 27, 1573-1574 (2011).
    • (2011) Bioinformatics , vol.27 , pp. 1573-1574
    • Vehlow, C.1
  • 43
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W., Dalke, A., Schulten, K. VMD: visual molecular dynamics. J. Mol. Graph. 14, 33-38, 27-28 (1996).
    • (1996) J. Mol. Graph. , vol.14 , Issue.33-38 , pp. 27-28
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 44
    • 0021895138 scopus 로고
    • A new generation of Ca2+ indicators with greatly improved fluorescence properties
    • Grynkiewicz, G., Poenie, M., Tsien, R.Y. A new generation of Ca2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 260, 3440-3450 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 45
    • 0028175559 scopus 로고
    • Ca2+ transport properties of ionophores A23187, ionomycin, and 4-BrA23187 in a well defined model system
    • Erdahl, W.L., Chapman, C.J., Taylor, R.W., Pfeiffer, D.R. Ca2+ transport properties of ionophores A23187, ionomycin, and 4-BrA23187 in a well defined model system. Biophys. J. 66, 1678-1693 (1994).
    • (1994) Biophys. J. , vol.66 , pp. 1678-1693
    • Erdahl, W.L.1    Chapman, C.J.2    Taylor, R.W.3    Pfeiffer, D.R.4
  • 47
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A.D. et al. All-atom empirical potential for molecular modeling and dynamics studies of proteins. J. Phys. Chem. B 102, 3586-3616 (1998).
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 48
    • 77958551193 scopus 로고    scopus 로고
    • APBSmem: A graphical interface for electrostatic calculations at the membrane
    • Callenberg, K.M. et al. APBSmem: a graphical interface for electrostatic calculations at the membrane. PLoS One 5, e12722 (2010).
    • (2010) PLoS One , vol.5 , pp. e12722
    • Callenberg, K.M.1
  • 49
    • 84946416234 scopus 로고    scopus 로고
    • GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers
    • Abraham, M.J. et al. GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX 1-2, 19-25 (2015).
    • (2015) SoftwareX , vol.1-2 , pp. 19-25
    • Abraham, M.J.1
  • 50
    • 84865723813 scopus 로고    scopus 로고
    • Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone ?, ? and side-chain ?1 and ?2 dihedral angles
    • Best, R.B. et al. Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone ?, ? and side-chain ?1 and ?2 dihedral angles. J. Chem. Theory Comput. 8, 3257-3273 (2012).
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 3257-3273
    • Best, R.B.1
  • 51
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations
    • Mackerell, A.D. Jr., Feig, M., Brooks, C.L. III. Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J. Comput. Chem. 25, 1400-1415 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1400-1415
    • MacKerell, Jr.A.D.1    Feig, M.2    Brooks, C.L.3
  • 53
    • 52949088587 scopus 로고    scopus 로고
    • Statistically optimal analysis of samples from multiple equilibrium states
    • Shirts, M.R., Chodera, J.D. Statistically optimal analysis of samples from multiple equilibrium states. J. Chem. Phys. 129, 124105 (2008).
    • (2008) J. Chem. Phys. , vol.129 , pp. 124105
    • Shirts, M.R.1    Chodera, J.D.2
  • 55
    • 49449113010 scopus 로고    scopus 로고
    • The MARTINI coarse-grained force field: Extension to proteins
    • Monticelli, L. et al. The MARTINI coarse-grained force field: extension to proteins. J. Chem. Theory Comput. 4, 819-834 (2008).
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 819-834
    • Monticelli, L.1
  • 57
    • 79955901803 scopus 로고    scopus 로고
    • Keep it flexible: Driving macromolecular rotary motions in atomistic simulations with GROMACS
    • Kutzner, C., Czub, J., Grubmüller, H. Keep it flexible: driving macromolecular rotary motions in atomistic simulations with GROMACS. J. Chem. Theory Comput. 7, 1381-1393 (2011).
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 1381-1393
    • Kutzner, C.1    Czub, J.2    Grubmüller, H.3


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