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Volumn 426, Issue 2, 2014, Pages 467-483

Structure of a prokaryotic sodium channel pore reveals essential gating elements and an outer ion binding site common to eukaryotic channels

Author keywords

electrophysiology; ion binding; voltage gated calcium channel; voltage gated sodium channel; X ray crystallography

Indexed keywords

ION; VOLTAGE GATED CALCIUM CHANNEL; VOLTAGE GATED SODIUM CHANNEL;

EID: 84891835113     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.10.010     Document Type: Article
Times cited : (122)

References (66)
  • 1
    • 0033694833 scopus 로고    scopus 로고
    • From ionic currents to molecular mechanisms: The structure and function of voltage-gated sodium channels
    • W.A. Catterall From ionic currents to molecular mechanisms: the structure and function of voltage-gated sodium channels Neuron 26 2000 13 25
    • (2000) Neuron , vol.26 , pp. 13-25
    • Catterall, W.A.1
  • 3
    • 77949300922 scopus 로고    scopus 로고
    • Voltage-gated sodium channels as therapeutic targets in epilepsy and other neurological disorders
    • M. Mantegazza, G. Curia, G. Biagini, D.S. Ragsdale, and M. Avoli Voltage-gated sodium channels as therapeutic targets in epilepsy and other neurological disorders Lancet Neurol 9 2010 413 424
    • (2010) Lancet Neurol , vol.9 , pp. 413-424
    • Mantegazza, M.1    Curia, G.2    Biagini, G.3    Ragsdale, D.S.4    Avoli, M.5
  • 4
    • 70349335964 scopus 로고    scopus 로고
    • Sodium channel blockers for the treatment of neuropathic pain
    • A. Bhattacharya, A.D. Wickenden, and S.R. Chaplan Sodium channel blockers for the treatment of neuropathic pain Neurotherapeutics 6 2009 663 678
    • (2009) Neurotherapeutics , vol.6 , pp. 663-678
    • Bhattacharya, A.1    Wickenden, A.D.2    Chaplan, S.R.3
  • 5
    • 77953293293 scopus 로고    scopus 로고
    • Paralytic shellfish poisoning: Seafood safety and human health perspectives
    • S.M. Etheridge Paralytic shellfish poisoning: seafood safety and human health perspectives Toxicon 56 2010 108 122
    • (2010) Toxicon , vol.56 , pp. 108-122
    • Etheridge, S.M.1
  • 6
    • 15244344363 scopus 로고    scopus 로고
    • The VGL-chanome: A protein superfamily specialized for electrical signaling and ionic homeostasis
    • F.H. Yu, and W.A. Catterall The VGL-chanome: a protein superfamily specialized for electrical signaling and ionic homeostasis Sci STKE 2004 2004 re15
    • (2004) Sci STKE , vol.2004 , pp. 15
    • Yu, F.H.1    Catterall, W.A.2
  • 7
    • 29844433234 scopus 로고    scopus 로고
    • Overview of molecular relationships in the voltage-gated ion channel superfamily
    • F.H. Yu, V. Yarov-Yarovoy, G.A. Gutman, and W.A. Catterall Overview of molecular relationships in the voltage-gated ion channel superfamily Pharmacol Rev 57 2005 387 395
    • (2005) Pharmacol Rev , vol.57 , pp. 387-395
    • Yu, F.H.1    Yarov-Yarovoy, V.2    Gutman, G.A.3    Catterall, W.A.4
  • 8
    • 0026517122 scopus 로고
    • Calcium channel characteristics conferred on the sodium channel by single mutations
    • S.H. Heinemann, H. Terlau, W. Stuhmer, K. Imoto, and S. Numa Calcium channel characteristics conferred on the sodium channel by single mutations Nature 356 1992 441 443
    • (1992) Nature , vol.356 , pp. 441-443
    • Heinemann, S.H.1    Terlau, H.2    Stuhmer, W.3    Imoto, K.4    Numa, S.5
  • 10
    • 0027430335 scopus 로고
    • Molecular localization of ion selectivity sites within the pore of a human L-type cardiac calcium channel
    • S. Tang, G. Mikala, A. Bahinski, A. Yatani, G. Varadi, and A. Schwartz Molecular localization of ion selectivity sites within the pore of a human L-type cardiac calcium channel J Biol Chem 268 1993 13026 13029
    • (1993) J Biol Chem , vol.268 , pp. 13026-13029
    • Tang, S.1    Mikala, G.2    Bahinski, A.3    Yatani, A.4    Varadi, G.5    Schwartz, A.6
  • 12
    • 1542364444 scopus 로고    scopus 로고
    • A superfamily of voltage-gated sodium channels in bacteria
    • R. Koishi, H. Xu, D. Ren, B. Navarro, B.W. Spiller, and Q. Shi et al. A superfamily of voltage-gated sodium channels in bacteria J Biol Chem 279 2004 9532 9538
    • (2004) J Biol Chem , vol.279 , pp. 9532-9538
    • Koishi, R.1    Xu, H.2    Ren, D.3    Navarro, B.4    Spiller, B.W.5    Shi, Q.6
  • 13
    • 77950463390 scopus 로고    scopus 로고
    • Comparative study of the gating motif and C-type inactivation in prokaryotic voltage-gated sodium channels
    • K. Irie, K. Kitagawa, H. Nagura, T. Imai, T. Shimomura, and Y. Fujiyoshi Comparative study of the gating motif and C-type inactivation in prokaryotic voltage-gated sodium channels J Biol Chem 285 2010 3685 3694
    • (2010) J Biol Chem , vol.285 , pp. 3685-3694
    • Irie, K.1    Kitagawa, K.2    Nagura, H.3    Imai, T.4    Shimomura, T.5    Fujiyoshi, Y.6
  • 14
    • 80051495437 scopus 로고    scopus 로고
    • NaChBac: The long lost sodium channel ancestor
    • K. Charalambous, and B.A. Wallace NaChBac: the long lost sodium channel ancestor Biochemistry 50 2011 6742 6752
    • (2011) Biochemistry , vol.50 , pp. 6742-6752
    • Charalambous, K.1    Wallace, B.A.2
  • 15
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • J. Payandeh, T. Scheuer, N. Zheng, and W.A. Catterall The crystal structure of a voltage-gated sodium channel Nature 475 2011 353 358
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 16
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • J. Payandeh, T.M. Gamal El-Din, T. Scheuer, N. Zheng, and W.A. Catterall Crystal structure of a voltage-gated sodium channel in two potentially inactivated states Nature 486 2012 135 139
    • (2012) Nature , vol.486 , pp. 135-139
    • Payandeh, J.1    Gamal El-Din, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 17
    • 84861952634 scopus 로고    scopus 로고
    • Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel
    • X. Zhang, W. Ren, P. DeCaen, C. Yan, X. Tao, and L. Tang et al. Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel Nature 486 2012 130 134
    • (2012) Nature , vol.486 , pp. 130-134
    • Zhang, X.1    Ren, W.2    Decaen, P.3    Yan, C.4    Tao, X.5    Tang, L.6
  • 18
    • 79955549892 scopus 로고    scopus 로고
    • A simplified bacterial "pore" provides insight into the assembly, stability and structure of sodium channels
    • E.C. McCusker, N. D'Avanzo, C.G. Nichols, and B.A. Wallace A simplified bacterial "Pore" provides insight into the assembly, stability and structure of sodium channels J Biol Chem 286 2011 16386 16391
    • (2011) J Biol Chem , vol.286 , pp. 16386-16391
    • McCusker, E.C.1    D'Avanzo, N.2    Nichols, C.G.3    Wallace, B.A.4
  • 19
    • 79961050460 scopus 로고    scopus 로고
    • Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins
    • D. Shaya, M. Kreir, R.A. Robbins, S. Wong, J. Hammon, and A. Bruggemann et al. Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins Proc Natl Acad Sci U S A 108 2011 12313 12318
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12313-12318
    • Shaya, D.1    Kreir, M.2    Robbins, R.A.3    Wong, S.4    Hammon, J.5    Bruggemann, A.6
  • 20
    • 84869478035 scopus 로고    scopus 로고
    • Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing
    • E.C. McCusker, C. Bagneris, C.E. Naylor, A.R. Cole, N. D'Avanzo, and C.G. Nichols et al. Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing Nat Commun 3 2012 1102
    • (2012) Nat Commun , vol.3 , pp. 1102
    • McCusker, E.C.1    Bagneris, C.2    Naylor, C.E.3    Cole, A.R.4    D'Avanzo, N.5    Nichols, C.G.6
  • 22
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • Z. Lu, A.M. Klem, and Y. Ramu Ion conduction pore is conserved among potassium channels Nature 413 2001 809 813
    • (2001) Nature , vol.413 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 28
    • 77956294944 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly
    • A.M. Powl, A.O. O'Reilly, A.J. Miles, and B.A. Wallace Synchrotron radiation circular dichroism spectroscopy-defined structure of the C-terminal domain of NaChBac and its role in channel assembly Proc Natl Acad Sci U S A 107 2010 14064 14069
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14064-14069
    • Powl, A.M.1    O'Reilly, A.O.2    Miles, A.J.3    Wallace, B.A.4
  • 29
    • 84860304780 scopus 로고    scopus 로고
    • The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate
    • K. Irie, T. Shimomura, and Y. Fujiyoshi The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate Nat Commun 3 2012 793
    • (2012) Nat Commun , vol.3 , pp. 793
    • Irie, K.1    Shimomura, T.2    Fujiyoshi, Y.3
  • 30
    • 77955269299 scopus 로고    scopus 로고
    • The C-terminal coiled-coil of the bacterial voltage-gated sodium channel NaChBac is not essential for tetramer formation, but stabilizes subunit-to-subunit interactions
    • K. Mio, M. Mio, F. Arisaka, M. Sato, and C. Sato The C-terminal coiled-coil of the bacterial voltage-gated sodium channel NaChBac is not essential for tetramer formation, but stabilizes subunit-to-subunit interactions Prog Biophys Mol Biol 103 2010 111 121
    • (2010) Prog Biophys Mol Biol , vol.103 , pp. 111-121
    • Mio, K.1    Mio, M.2    Arisaka, F.3    Sato, M.4    Sato, C.5
  • 31
    • 0023070561 scopus 로고
    • Molecular properties of ion permeation through sodium channels
    • T. Begenisich Molecular properties of ion permeation through sodium channels Annu Rev Biophys Biophys Chem 16 1987 247 263
    • (1987) Annu Rev Biophys Biophys Chem , vol.16 , pp. 247-263
    • Begenisich, T.1
  • 34
    • 0021280815 scopus 로고
    • Mechanism of ion permeation through calcium channels
    • P. Hess, and R.W. Tsien Mechanism of ion permeation through calcium channels Nature 309 1984 453 456
    • (1984) Nature , vol.309 , pp. 453-456
    • Hess, P.1    Tsien, R.W.2
  • 35
    • 84874661354 scopus 로고    scopus 로고
    • Analysis of the selectivity filter of the voltage-gated sodium channel Na(v)Rh
    • X. Zhang, M. Xia, Y. Li, H. Liu, X. Jiang, and W. Ren et al. Analysis of the selectivity filter of the voltage-gated sodium channel Na(v)Rh Cell Res 23 2012 409 422
    • (2012) Cell Res , vol.23 , pp. 409-422
    • Zhang, X.1    Xia, M.2    Li, Y.3    Liu, H.4    Jiang, X.5    Ren, W.6
  • 36
    • 84856737491 scopus 로고    scopus 로고
    • Sodium ion binding sites and hydration in the lumen of a bacterial ion channel from molecular dynamics simulations
    • V. Carnevale, W. Treptow, and M.L. Klein Sodium ion binding sites and hydration in the lumen of a bacterial ion channel from molecular dynamics simulations J Phys Chem Lett 2 2011 2504 2508
    • (2011) J Phys Chem Lett , vol.2 , pp. 2504-2508
    • Carnevale, V.1    Treptow, W.2    Klein, M.L.3
  • 37
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • P.A. Karplus, and K. Diederichs Linking crystallographic model and data quality Science 336 2012 1030 1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 41
    • 33847091589 scopus 로고    scopus 로고
    • Structural insight into KCNQ (Kv7) channel assembly and channelopathy
    • R.J. Howard, K.A. Clark, J.M. Holton, and D.L. Minor Structural insight into KCNQ (Kv7) channel assembly and channelopathy Neuron 53 2007 663 675
    • (2007) Neuron , vol.53 , pp. 663-675
    • Howard, R.J.1    Clark, K.A.2    Holton, J.M.3    Minor, D.L.4
  • 42
    • 41949105973 scopus 로고    scopus 로고
    • The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit assembly and protein interaction
    • R. Wiener, Y. Haitin, L. Shamgar, M.C. Fernandez-Alonso, A. Martos, and O. Chomsky-Hecht et al. The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit assembly and protein interaction J Biol Chem 283 2008 5815 5830
    • (2008) J Biol Chem , vol.283 , pp. 5815-5830
    • Wiener, R.1    Haitin, Y.2    Shamgar, L.3    Fernandez-Alonso, M.C.4    Martos, A.5    Chomsky-Hecht, O.6
  • 43
    • 33745877323 scopus 로고    scopus 로고
    • Coiled coils direct assembly of a cold-activated TRP channel
    • P.R. Tsuruda, D. Julius, and D.L. Minor Coiled coils direct assembly of a cold-activated TRP channel Neuron 51 2006 201 212
    • (2006) Neuron , vol.51 , pp. 201-212
    • Tsuruda, P.R.1    Julius, D.2    Minor, D.L.3
  • 46
    • 0034856791 scopus 로고    scopus 로고
    • Structural characteristics of protein binding sites for calcium and lanthanide ions
    • E. Pidcock, and G.R. Moore Structural characteristics of protein binding sites for calcium and lanthanide ions J Biol Inorg Chem 6 2001 479 489
    • (2001) J Biol Inorg Chem , vol.6 , pp. 479-489
    • Pidcock, E.1    Moore, G.R.2
  • 47
    • 48849104435 scopus 로고    scopus 로고
    • Data mining of metal ion environments present in protein structures
    • H. Zheng, M. Chruszcz, P. Lasota, L. Lebioda, and W. Minor Data mining of metal ion environments present in protein structures J Inorg Biochem 102 2008 1765 1776
    • (2008) J Inorg Biochem , vol.102 , pp. 1765-1776
    • Zheng, H.1    Chruszcz, M.2    Lasota, P.3    Lebioda, L.4    Minor, W.5
  • 48
    • 0036899251 scopus 로고    scopus 로고
    • The cation selectivity filter of the bacterial sodium channel, NaChBac
    • L. Yue, B. Navarro, D. Ren, A. Ramos, and D.E. Clapham The cation selectivity filter of the bacterial sodium channel, NaChBac J Gen Physiol 120 2002 845 853
    • (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
  • 50
    • 64549106513 scopus 로고    scopus 로고
    • Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation
    • F. Findeisen, and D.L. Minor Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation J Gen Physiol 133 2009 327 343
    • (2009) J Gen Physiol , vol.133 , pp. 327-343
    • Findeisen, F.1    Minor, D.L.2
  • 51
    • 84864885076 scopus 로고    scopus 로고
    • Metabolic and thermal stimuli control K(2P)2.1 (TREK-1) through modular sensory and gating domains
    • S.N. Bagriantsev, K.A. Clark, and D.L. Minor Metabolic and thermal stimuli control K(2P)2.1 (TREK-1) through modular sensory and gating domains EMBO J 31 2012 3297 3308
    • (2012) EMBO J , vol.31 , pp. 3297-3308
    • Bagriantsev, S.N.1    Clark, K.A.2    Minor, D.L.3
  • 52
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • K.T. O'Neil, and W.F. DeGrado A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids Science 250 1990 646 651
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    Degrado, W.F.2
  • 54
    • 84872121904 scopus 로고    scopus 로고
    • Structure of a Ca(2 +)/CaM:Kv7.4 (KCNQ4) B-helix complex provides insight into M current modulation
    • Q. Xu, A. Chang, A. Tolia, and D.L. Minor Structure of a Ca(2 +)/CaM:Kv7.4 (KCNQ4) B-helix complex provides insight into M current modulation J Mol Biol 425 2013 378 394
    • (2013) J Mol Biol , vol.425 , pp. 378-394
    • Xu, Q.1    Chang, A.2    Tolia, A.3    Minor, D.L.4
  • 55
    • 44149126774 scopus 로고    scopus 로고
    • The C-terminus of Kv7 channels: A multifunctional module
    • Y. Haitin, and B. Attali The C-terminus of Kv7 channels: a multifunctional module J Physiol 586 2008 1803 1810
    • (2008) J Physiol , vol.586 , pp. 1803-1810
    • Haitin, Y.1    Attali, B.2
  • 56
    • 23244467740 scopus 로고    scopus 로고
    • The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel
    • E. Pavlov, C. Bladen, R. Winkfein, C. Diao, P. Dhaliwal, and R.J. French The pore, not cytoplasmic domains, underlies inactivation in a prokaryotic sodium channel Biophys J 89 2005 232 242
    • (2005) Biophys J , vol.89 , pp. 232-242
    • Pavlov, E.1    Bladen, C.2    Winkfein, R.3    Diao, C.4    Dhaliwal, P.5    French, R.J.6
  • 60
    • 77953714921 scopus 로고    scopus 로고
    • Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels
    • O.B. Clarke, A.T. Caputo, A.P. Hill, J.I. Vandenberg, B.J. Smith, and J.M. Gulbis Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels Cell 141 2010 1018 1029
    • (2010) Cell , vol.141 , pp. 1018-1029
    • Clarke, O.B.1    Caputo, A.T.2    Hill, A.P.3    Vandenberg, J.I.4    Smith, B.J.5    Gulbis, J.M.6
  • 62
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: Space-group determination, scaling and intensity statistics
    • P.R. Evans An introduction to data reduction: space-group determination, scaling and intensity statistics Acta Crystallogr Sect D Biol Crystallogr 67 2011 282 292
    • (2011) Acta Crystallogr Sect D Biol Crystallogr , vol.67 , pp. 282-292
    • Evans, P.R.1
  • 65
    • 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 Sect D Biol Crystallogr 50 1994 760 763
    • (1994) Acta Crystallogr Sect D Biol Crystallogr , vol.50 , pp. 760-763
  • 66
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • O.P. Hamill, A. Marty, E. Neher, B. Sakmann, and F.J. Sigworth Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches Pflugers Arch 391 1981 85 100
    • (1981) Pflugers Arch , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5


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