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Volumn 486, Issue 7401, 2012, Pages 130-134

Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CALCIUM ION; OXYGEN; PROTEIN NACHBAC; PROTEIN NAVRH; SODIUM ION; TETRAMER; UNCLASSIFIED DRUG; VOLTAGE GATED SODIUM CHANNEL;

EID: 84861952634     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11054     Document Type: Article
Times cited : (416)

References (47)
  • 2
    • 77949300922 scopus 로고    scopus 로고
    • Voltage-gated sodium channels as therapeutic targets in epilepsy and other neurological disorders
    • Mantegazza, M., Curia, G., Biagini, G., Ragsdale, D. S. & Avoli, M. Voltage-gated sodium channels as therapeutic targets in epilepsy and other neurological disorders. Lancet Neurol. 9, 413-424 (2010).
    • (2010) Lancet Neurol. , vol.9 , pp. 413-424
    • Mantegazza, M.1    Curia, G.2    Biagini, G.3    Ragsdale, D.S.4    Avoli, M.5
  • 3
    • 0035861457 scopus 로고    scopus 로고
    • A prokaryotic voltage-gated sodium channel
    • Ren, D. et al. A prokaryotic voltage-gated sodium channel. Science 294, 2372-2375 (2001).
    • (2001) Science , vol.294 , pp. 2372-2375
    • Ren, D.1
  • 4
    • 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
  • 5
    • 0021330126 scopus 로고
    • Themolecular basis of neuronal excitability
    • Catterall, W. A. Themolecular basis of neuronal excitability. Science 223, 653-661 (1984).
    • (1984) Science , vol.223 , pp. 653-661
    • Catterall, W.A.1
  • 6
    • 0038076054 scopus 로고    scopus 로고
    • X-ray structure of a voltage-dependent K1 channel
    • Jiang, Y. et al. X-ray structure of a voltage-dependent K1 channel. Nature 423, 33-41 (2003).
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1
  • 7
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • Long, S. B., Campbell, E. B. & Mackinnon, R. Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908 (2005).
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 8
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltagedependent K1 channel in a lipid membrane-like environment
    • Long, S. B., Tao, X., Campbell, E. B. & MacKinnon, R. Atomic structure of a voltagedependent K1 channel in a lipid membrane-like environment. Nature 450, 376-382 (2007).
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 9
    • 77957924708 scopus 로고    scopus 로고
    • Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP
    • Butterwick, J. A.& MacKinnon, R. Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP. J. Mol. Biol. 403, 591-606 (2010).
    • (2010) J. Mol. Biol. , vol.403 , pp. 591-606
    • Butterwick, J.A.1    MacKinnon, R.2
  • 10
    • 0016354136 scopus 로고
    • Charge movement associated with the opening and closing of the activation gates of the Na channels
    • Armstrong, C. M. & Bezanilla, F. Charge movement associated with the opening and closing of the activation gates of the Na channels. J. Gen. Physiol. 63, 533-552 (1974).
    • (1974) J. Gen. Physiol. , vol.63 , pp. 533-552
    • Armstrong, C.M.1    Bezanilla, F.2
  • 11
    • 0030175348 scopus 로고    scopus 로고
    • Contribution of the S4segment to gating charge in the Shaker K1 channel
    • Aggarwal, S. K.&MacKinnon, R.Contribution of the S4segment to gating charge in the Shaker K1 channel. Neuron 16, 1169-1177 (1996).
    • (1996) Neuron , vol.16 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 12
    • 0030175867 scopus 로고    scopus 로고
    • Voltage-sensing residues in the S2 and S4 segments of the Shaker K1 channel
    • Seoh, S. A., Sigg, D., Papazian, D. M. & Bezanilla, F. Voltage-sensing residues in the S2 and S4 segments of the Shaker K1 channel. Neuron 16, 1159-1167 (1996).
    • (1996) Neuron , vol.16 , pp. 1159-1167
    • Seoh, S.A.1    Sigg, D.2    Papazian, D.M.3    Bezanilla, F.4
  • 13
    • 0023784649 scopus 로고
    • Identification of an intracellularpeptide segment involved in sodium channel inactivation
    • Vassilev, P. M., Scheuer, T.&Catterall, W. A. Identification of an intracellularpeptide segment involved in sodium channel inactivation. Science 241, 1658-1661 (1988).
    • (1988) Science , vol.241 , pp. 1658-1661
    • Vassilev, P.M.1    Scheuer, T.2    Catterall, W.A.3
  • 14
    • 0015868742 scopus 로고
    • Currents related to movement of the gating particles of the sodium channels
    • Armstrong, C. M. & Bezanilla, F. Currents related to movement of the gating particles of the sodium channels. Nature 242, 459-461 (1973).
    • (1973) Nature , vol.242 , pp. 459-461
    • Armstrong, C.M.1    Bezanilla, F.2
  • 15
    • 0025224223 scopus 로고
    • Biophysical andmolecularmechanisms of Shaker potassium channel inactivation
    • Hoshi, T., Zagotta, W. N.& Aldrich, R. W. Biophysical andmolecularmechanisms of Shaker potassium channel inactivation. Science 250, 533-538 (1990).
    • (1990) Science , vol.250 , pp. 533-538
    • Hoshi, T.1    Zagotta, W.N.2    Aldrich, R.W.3
  • 16
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassiumchannels by a peptide derived fromShB
    • Zagotta, W. N., Hoshi, T. & Aldrich, R. W. Restoration of inactivation in mutants of Shaker potassiumchannels by a peptide derived fromShB. Science 250, 568-571 (1990).
    • (1990) Science , vol.250 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 17
    • 25444498065 scopus 로고    scopus 로고
    • Sodium channel inactivation: Molecular determinants and modulation
    • Ulbricht, W. Sodium channel inactivation: molecular determinants and modulation. Physiol. Rev. 85, 1271-1301 (2005).
    • (2005) Physiol. Rev. , vol.85 , pp. 1271-1301
    • Ulbricht, W.1
  • 18
    • 0032982292 scopus 로고    scopus 로고
    • Ultra-slow inactivation in mu1 Na1 channels is produced by a structural rearrangement of the outer vestibule
    • Todt, H., Dudley, S. C. Jr, Kyle, J. W., French, R. J. & Fozzard, H. A. Ultra-slow inactivation in mu1 Na1 channels is produced by a structural rearrangement of the outer vestibule. Biophys. J. 76, 1335-1345 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 1335-1345
    • Todt, H.1    Dudley Jr., S.C.2    Kyle, J.W.3    French, R.J.4    Fozzard, H.A.5
  • 19
    • 0028297301 scopus 로고
    • An engineered cysteine in the external mouth of a K1 channel allows inactivation to be modulated by metal binding
    • Yellen, G., Sodickson, D., Chen, T. Y. & Jurman, M. E. An engineered cysteine in the external mouth of a K1 channel allows inactivation to be modulated by metal binding. Biophys. J. 66, 1068-1075 (1994).
    • (1994) Biophys. J. , vol.66 , pp. 1068-1075
    • Yellen, G.1    Sodickson, D.2    Chen, T.Y.3    Jurman, M.E.4
  • 20
    • 0034806053 scopus 로고    scopus 로고
    • A putative prokaryote voltage-gated Ca21 channel with only one 6TM motif per subunit
    • Durell, S. R. & Guy, H. R. A putative prokaryote voltage-gated Ca21 channel with only one 6TM motif per subunit. Biochem. Biophys. Res. Commun. 281, 741-746 (2001).
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 741-746
    • Durell, S.R.1    Guy, H.R.2
  • 21
    • 0036899251 scopus 로고    scopus 로고
    • The cation selectivity filter of the bacterial sodium channel, NaChBac
    • Yue, L.,Navarro, B., Ren, D., Ramos, A.&Clapham, D. E. The cation selectivity filter of the bacterial sodium channel, NaChBac. J. Gen. Physiol. 120, 845-853 (2002).
    • (2002) J. Gen. Physiol. , vol.120 , pp. 845-853
    • Yue, L.1    Navarro, B.2    Ren, D.3    Ramos, A.4    Clapham, D.E.5
  • 22
    • 23244467740 scopus 로고    scopus 로고
    • The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel
    • Pavlov, E. et al. The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel. Biophys. J. 89, 232-242 (2005).
    • (2005) Biophys. J. , vol.89 , pp. 232-242
    • Pavlov, E.1
  • 23
    • 0033179802 scopus 로고    scopus 로고
    • The geometry of metal-ligandinteractions relevant to proteins
    • Harding, M. M. The geometry of metal-ligandinteractions relevant to proteins. Acta Crystallogr. D 55, 1432-1443 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1432-1443
    • Harding, M.M.1
  • 24
    • 84944648082 scopus 로고
    • Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides
    • Shannon, R. D. Revised effective ionic radii and systematic studies of interatomic distances in halides and chalcogenides. Acta Crystallogr. A 32, 751-767 (1976).
    • (1976) Acta Crystallogr. A , vol.32 , pp. 751-767
    • Shannon, R.D.1
  • 25
    • 0015009509 scopus 로고
    • The hydration of sodium ions crossing the nerve membrane
    • Hille, B. The hydration of sodium ions crossing the nerve membrane. Proc. Natl Acad. Sci. USA 68, 280-282 (1971).
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , pp. 280-282
    • Hille, B.1
  • 26
    • 0026077570 scopus 로고
    • Calcium ion as a cofactor in Na channel gating
    • Armstrong, C. M. & Cota, G. Calcium ion as a cofactor in Na channel gating. Proc. Natl Acad. Sci. USA 88, 6528-6531 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 6528-6531
    • Armstrong, C.M.1    Cota, G.2
  • 27
    • 67649867931 scopus 로고    scopus 로고
    • A gating model for the archeal voltagedependent K1 channel KvAP in DPhPC and POPE:POPG decane lipid bilayers
    • Schmidt, D., Cross, S. R. & MacKinnon, R. A gating model for the archeal voltagedependent K1 channel KvAP in DPhPC and POPE:POPG decane lipid bilayers. J. Mol. Biol. 390, 902-912 (2009).
    • (2009) J. Mol. Biol. , vol.390 , pp. 902-912
    • Schmidt, D.1    Cross, S.R.2    MacKinnon, R.3
  • 28
    • 0141513676 scopus 로고    scopus 로고
    • Molecular motions of the outer ring of charge of the sodiumchannel: Do they couple to slow inactivation?
    • Xiong, W., Li, R. A., Tian, Y. & Tomaselli, G. F. Molecular motions of the outer ring of charge of the sodiumchannel: do they couple to slow inactivation? J. Gen. Physiol. 122, 323-332 (2003).
    • (2003) J. Gen. Physiol. , vol.122 , pp. 323-332
    • Xiong, W.1    Li, R.A.2    Tian, Y.3    Tomaselli, G.F.4
  • 31
    • 0028136070 scopus 로고
    • Crystal structure of rat DNA polymerase beta: Evidence for a common polymerase mechanism
    • Sawaya,M. R., Pelletier, H., Kumar, A., Wilson, S. H.&Kraut, J. Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism. Science 264, 1930-1935 (1994).
    • (1994) Science , vol.264 , pp. 1930-1935
    • Sawayam, R.1    Pelletier, H.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 35
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658-674 (2007).
    • (2007) J. Appl. Cryst. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 37
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 38
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 39
    • 40849122470 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system
    • DeLano, W. L. The PyMOL Molecular Graphics System. Pymol http://www.pymol.org (2002).
    • (2002) Pymol
    • Delano, W.L.1
  • 41
    • 32144432437 scopus 로고    scopus 로고
    • TheSWISS-MODEL workspace: Awebbased environment for protein structure homology modelling
    • Arnold, K., Bordoli, L.,Kopp, J.&Schwede, T. TheSWISS-MODEL workspace: awebbased environment for protein structure homology modelling. Bioinformatics 22, 195-201 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 42
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N. & Peitsch, M. C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 43
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 44
    • 0037246863 scopus 로고    scopus 로고
    • MolMovDB: Analysis and visualization of conformational change and structural flexibility
    • Echols, N., Milburn, D. & Gerstein, M. MolMovDB: analysis and visualization of conformational change and structural flexibility. Nucleic Acids Res. 31, 478-482 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 478-482
    • Echols, N.1    Milburn, D.2    Gerstein, M.3
  • 45
    • 0034655949 scopus 로고    scopus 로고
    • Themorph server: A standardized systemfor analyzing and visualizing macromolecular motions in a database framework
    • Krebs, W. G.& Gerstein, M. Themorph server: a standardized systemfor analyzing and visualizing macromolecular motions in a database framework. Nucleic Acids Res. 28, 1665-1675 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1665-1675
    • Krebs, W.G.1    Gerstein, M.2
  • 46
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR System: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR System: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 47
    • 37049014272 scopus 로고    scopus 로고
    • Version1.2 of the Crystallography and NMR system
    • Brunger, A. T.Version1.2 of the Crystallography andNMRsystem.Nature Protocols 2, 2728-2733 (2007).
    • (2007) Nature Protocols , vol.2 , pp. 2728-2733
    • Brunger, A.T.1


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