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Volumn 516, Issue 7530, 2014, Pages 207-212

X-ray structure of a calcium-activated TMEM16 lipid scramblase

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ACTIVATED CHLORIDE CHANNEL; DIMER; FUNGAL PROTEIN; SCRAMBLASE; TMEM16 PROTEIN; UNCLASSIFIED DRUG; ANO1 PROTEIN, HUMAN; CALCIUM; CHLORIDE CHANNEL; LIPID BILAYER; PHOSPHOLIPID TRANSFER PROTEIN; PROTEIN SUBUNIT; TUMOR PROTEIN;

EID: 84918807150     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13984     Document Type: Article
Times cited : (369)

References (67)
  • 1
    • 77958051307 scopus 로고    scopus 로고
    • Evolution and functional divergence of the anoctamin family of membrane proteins
    • Milenkovic, V. M., Brockmann, M., Stohr, H.,Weber, B. H.&Strauss, O. Evolution and functional divergence of the anoctamin family of membrane proteins. BMC Evol. Biol. 10, 319 (2010).
    • (2010) BMC Evol. Biol. , vol.10 , pp. 319
    • Milenkovic, V.M.1    Brockmann, M.2    Stohr, H.3    Weber, B.H.4    Strauss, O.5
  • 2
    • 84900406113 scopus 로고    scopus 로고
    • Structure and function of TMEM16 proteins (anoctamins)
    • Pedemonte, N. & Galietta, L. J. Structure and function of TMEM16 proteins (anoctamins). Physiol. Rev. 94, 419-459 (2014).
    • (2014) Physiol. Rev. , vol.94 , pp. 419-459
    • Pedemonte, N.1    Galietta, L.J.2
  • 3
    • 55249091085 scopus 로고    scopus 로고
    • TMEM16Aconfers receptor-activatedcalcium-dependent chloride conductance
    • Yang, Y. D. et al.TMEM16Aconfers receptor-activatedcalcium-dependent chloride conductance. Nature 455, 1210-1215 (2008).
    • (2008) Nature , vol.455 , pp. 1210-1215
    • Yang, Y.D.1
  • 4
    • 54949112835 scopus 로고    scopus 로고
    • TMEM16A, a membrane protein associated with calciumdependent chloride channel activity
    • Caputo, A. et al. TMEM16A, a membrane protein associated with calciumdependent chloride channel activity. Science 322, 590-594 (2008).
    • (2008) Science , vol.322 , pp. 590-594
    • Caputo, A.1
  • 5
    • 51549120559 scopus 로고    scopus 로고
    • Expression cloning ofTMEM16A as a calcium-activated chloride channel subunit
    • Schroeder, B. C., Cheng, T., Jan, Y. N.&Jan, L. Y. Expression cloning ofTMEM16A as a calcium-activated chloride channel subunit. Cell 134, 1019-1029 (2008).
    • (2008) Cell , vol.134 , pp. 1019-1029
    • Schroeder, B.C.1    Cheng, T.2    Jan, Y.N.3    Jan, L.Y.4
  • 6
    • 84856431269 scopus 로고    scopus 로고
    • Anoctamin 2/TMEM16B: A calcium-activated chloride channel in olfactory transduction
    • Pifferi, S., Cenedese, V. & Menini, A. Anoctamin 2/TMEM16B: a calcium-activated chloride channel in olfactory transduction. Exp. Physiol. 97, 193-199 (2012).
    • (2012) Exp. Physiol. , vol.97 , pp. 193-199
    • Pifferi, S.1    Cenedese, V.2    Menini, A.3
  • 8
    • 83455199984 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. LXXXV: Calcium-activated chloride channels
    • Huang, F., Wong, X. & Jan, L. Y. International Union of Basic and Clinical Pharmacology. LXXXV: calcium-activated chloride channels. Pharmacol. Rev. 64, 1-15 (2012).
    • (2012) Pharmacol. Rev. , vol.64 , pp. 1-15
    • Huang, F.1    Wong, X.2    Jan, L.Y.3
  • 9
    • 79960843311 scopus 로고    scopus 로고
    • Ca21-activated Cl-currents are dispensable for olfaction
    • Billig, G. M., Pal, B., Fidzinski, P. & Jentsch, T. J. Ca21-activated Cl-currents are dispensable for olfaction. Nature Neurosci. 14, 763-769 (2011).
    • (2011) Nature Neurosci. , vol.14 , pp. 763-769
    • Billig, G.M.1    Pal, B.2    Fidzinski, P.3    Jentsch, T.J.4
  • 10
    • 84871860558 scopus 로고    scopus 로고
    • TMEM16F forms a Ca21-activated cation channel required for lipid scrambling in platelets during blood coagulation
    • Yang, H. et al. TMEM16F forms a Ca21-activated cation channel required for lipid scrambling in platelets during blood coagulation. Cell 151, 111-122 (2012).
    • (2012) Cell , vol.151 , pp. 111-122
    • Yang, H.1
  • 11
    • 81055126222 scopus 로고    scopus 로고
    • Anoctamin 6 is an essential component of the outwardly rectifying chloride channel
    • Martins, J. R. et al. Anoctamin 6 is an essential component of the outwardly rectifying chloride channel. Proc. Natl Acad. Sci. USA 108, 18168-18172 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 18168-18172
    • Martins, J.R.1
  • 12
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • Suzuki, J., Umeda, M., Sims, P. J. & Nagata, S. Calcium-dependent phospholipid scrambling by TMEM16F. Nature 468, 834-838 (2010).
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 13
    • 84877709762 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members
    • Suzuki, J. et al. Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members. J. Biol. Chem. 288, 13305-13316 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 13305-13316
    • Suzuki, J.1
  • 14
    • 84884144976 scopus 로고    scopus 로고
    • Ca21-dependent phospholipid scrambling by a reconstituted TMEM16 ion channel
    • Malvezzi, M. et al. Ca21-dependent phospholipid scrambling by a reconstituted TMEM16 ion channel. Nature Commun. 4, 2367 (2013).
    • (2013) Nature Commun. , vol.4 , pp. 2367
    • Malvezzi, M.1
  • 15
    • 84896711031 scopus 로고    scopus 로고
    • Molecular functions of anoctamin 6 (TMEM16F): A chloride channel, cation channel, or phospholipid scramblase?
    • Kunzelmann, K. et al. Molecular functions of anoctamin 6 (TMEM16F): a chloride channel, cation channel, or phospholipid scramblase? Pflugers Arch. 466, 407-414 (2014).
    • (2014) Pflugers Arch. , vol.466 , pp. 407-414
    • Kunzelmann, K.1
  • 16
    • 0033971365 scopus 로고    scopus 로고
    • Bimodal control of a Ca21-activated Cl2 channel by different Ca21 signals
    • Kuruma, A. & Hartzell, H. C. Bimodal control of a Ca21-activated Cl2 channel by different Ca21 signals. J. Gen. Physiol. 115, 59-80 (2000).
    • (2000) J. Gen. Physiol. , vol.115 , pp. 59-80
    • Kuruma, A.1    Hartzell, H.C.2
  • 17
    • 84900460157 scopus 로고    scopus 로고
    • Activation and inhibition of TMEM16A calcium-activated chloride channels
    • Ni, Y. L., Kuan, A. S. & Chen, T. Y. Activation and inhibition of TMEM16A calcium-activated chloride channels. PLoS ONE 9, e86734 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e86734
    • Ni, Y.L.1    Kuan, A.S.2    Chen, T.Y.3
  • 18
    • 84859435658 scopus 로고    scopus 로고
    • Explaining calcium-dependent gating of anoctamin-1 chloride channels requires a revised topology
    • Yu, K., Duran, C., Qu, Z., Cui, Y. Y. & Hartzell, H. C. Explaining calcium-dependent gating of anoctamin-1 chloride channels requires a revised topology. Circ. Res. 110, 990-999 (2012).
    • (2012) Circ. Res. , vol.110 , pp. 990-999
    • Yu, K.1    Duran, C.2    Qu, Z.3    Cui, Y.Y.4    Hartzell, H.C.5
  • 19
    • 84888323395 scopus 로고    scopus 로고
    • Purified TMEM16A is sufficient to form Ca21-activated Cl-channels
    • Terashima, H., Picollo, A. & Accardi, A. Purified TMEM16A is sufficient to form Ca21-activated Cl-channels. Proc. Natl Acad. Sci. USA 110, 19354-19359 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 19354-19359
    • Terashima, H.1    Picollo, A.2    Accardi, A.3
  • 20
    • 79151482289 scopus 로고    scopus 로고
    • Opsin is a phospholipid flippase
    • Menon, I. et al. Opsin is a phospholipid flippase. Curr. Biol. 21, 149-153 (2011).
    • (2011) Curr. Biol. , vol.21 , pp. 149-153
    • Menon, I.1
  • 21
    • 84905186544 scopus 로고    scopus 로고
    • A comprehensive search for calcium binding sites critical for TMEM16A calcium-activated chloride channel activity
    • Tien, J. et al. A comprehensive search for calcium binding sites critical for TMEM16A calcium-activated chloride channel activity. eLife 3, e02772 (2014).
    • (2014) ELife , vol.3 , pp. e02772
    • Tien, J.1
  • 22
    • 79953195560 scopus 로고    scopus 로고
    • TMEM16A(a)/anoctamin-1shares a homodimeric architecture with CLC chloride channels
    • Fallah, G. et al.TMEM16A(a)/anoctamin-1shares a homodimeric architecture with CLC chloride channels. Mol. Cell. Proteomics 10, M110.004697 (2011).
    • (2011) Mol. Cell. Proteomics , vol.10 , pp. M110004697
    • Fallah, G.1
  • 23
    • 78651384517 scopus 로고    scopus 로고
    • Characterization of the oligomeric structure of the Ca21-activated Cl-channel Ano1/TMEM16A
    • Sheridan, J. T. et al. Characterization of the oligomeric structure of the Ca21-activated Cl-channel Ano1/TMEM16A. J. Biol. Chem. 286, 1381-1388 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 1381-1388
    • Sheridan, J.T.1
  • 24
    • 84876232419 scopus 로고    scopus 로고
    • Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC)
    • Tien, J., Lee, H. Y., Minor, D. L. Jr, Jan, Y. N.&Jan, L. Y. Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC). Proc. Natl Acad. Sci. USA 110, 6352-6357 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 6352-6357
    • Tien, J.1    Lee, H.Y.2    Minor, D.L.3    Jan, Y.N.4    Jan, L.Y.5
  • 25
    • 65749107370 scopus 로고    scopus 로고
    • Anoctamin/TMEM16 family members are Ca21-activated Cl2 channels
    • Hartzell, H. C., Yu, K., Xiao, Q., Chien, L. T. & Qu, Z. Anoctamin/TMEM16 family members are Ca21-activated Cl2 channels. J. Physiol. (Lond.) 587, 2127-2139 (2009).
    • (2009) J. Physiol. (Lond.) , vol.587 , pp. 2127-2139
    • Hartzell, H.C.1    Yu, K.2    Xiao, Q.3    Chien, L.T.4    Qu, Z.5
  • 26
    • 73449119238 scopus 로고    scopus 로고
    • Flipping lipids: Why an' what's the reason for?
    • Sanyal, S. & Menon, A. K. Flipping lipids: why an' what's the reason for? ACS Chem. Biol. 4, 895-909 (2009).
    • (2009) ACS Chem. Biol. , vol.4 , pp. 895-909
    • Sanyal, S.1    Menon, A.K.2
  • 27
    • 84880758440 scopus 로고    scopus 로고
    • Xk-related protein 8 and CED-8 promote phosphatidylserine exposure in apoptotic cells
    • Suzuki, J., Denning, D. P., Imanishi, E., Horvitz, H. R. & Nagata, S. Xk-related protein 8 and CED-8 promote phosphatidylserine exposure in apoptotic cells. Science 341, 403-406 (2013).
    • (2013) Science , vol.341 , pp. 403-406
    • Suzuki, J.1    Denning, D.P.2    Imanishi, E.3    Horvitz, H.R.4    Nagata, S.5
  • 28
    • 77954947798 scopus 로고    scopus 로고
    • Stereoselective transbilayer translocation of mannosyl phosphoryl dolichol by an endoplasmic reticulum flippase
    • Sanyal, S. & Menon, A. K. Stereoselective transbilayer translocation of mannosyl phosphoryl dolichol by an endoplasmic reticulum flippase. Proc. Natl Acad. Sci. USA 107, 11289-11294 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 11289-11294
    • Sanyal, S.1    Menon, A.K.2
  • 29
    • 79955007775 scopus 로고    scopus 로고
    • Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane
    • Mohammadi, T. et al. Identification of FtsW as a transporter of lipid-linked cell wall precursors across the membrane. EMBO J. 30, 1425-1432 (2011).
    • (2011) EMBO J. , vol.30 , pp. 1425-1432
    • Mohammadi, T.1
  • 30
    • 2942637935 scopus 로고    scopus 로고
    • Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids
    • Zwaal, R. F., Comfurius, P. & Bevers, E. M. Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids. Biochim. Biophys. Acta 1636, 119-128 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1636 , pp. 119-128
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 31
    • 0037085646 scopus 로고    scopus 로고
    • Comparison between Ca21-induced scrambling of various fluorescently labelled lipid analogues in red blood cells
    • Dekkers, D. W., Comfurius, P., Bevers, E. M. & Zwaal, R. F. Comparison between Ca21-induced scrambling of various fluorescently labelled lipid analogues in red blood cells. Biochem. J. 362, 741-747 (2002).
    • (2002) Biochem. J. , vol.362 , pp. 741-747
    • Dekkers, D.W.1    Comfurius, P.2    Bevers, E.M.3    Zwaal, R.F.4
  • 32
    • 84904097466 scopus 로고    scopus 로고
    • Bacterial cellwall.MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis
    • Sham,L. T. et al.Bacterial cellwall.MurJ is the flippase of lipid-linked precursors for peptidoglycan biogenesis. Science 345, 220-222 (2014).
    • (2014) Science , vol.345 , pp. 220-222
    • Sham, L.T.1
  • 33
    • 84896291266 scopus 로고    scopus 로고
    • Functional swapping between transmembrane proteins TMEM16A and TMEM16F
    • Suzuki, T., Suzuki, J. & Nagata, S. Functional swapping between transmembrane proteins TMEM16A and TMEM16F. J. Biol. Chem. 289, 7438-7447 (2014).
    • (2014) J. Biol. Chem. , vol.289 , pp. 7438-7447
    • Suzuki, T.1    Suzuki, J.2    Nagata, S.3
  • 34
    • 0020440405 scopus 로고
    • Open-state substructure of single chloride channels from Torpedo electroplax
    • Miller, C. Open-state substructure of single chloride channels from Torpedo electroplax. Phil. Trans. R. Soc. Lond. B 299, 401-411 (1982).
    • (1982) Phil. Trans. R. Soc. Lond. B , vol.299 , pp. 401-411
    • Miller, C.1
  • 35
    • 84876925080 scopus 로고    scopus 로고
    • Calcium-activated and apoptotic phospholipid scrambling induced by Ano6 can occur independently of Ano6 ion currents
    • Kmit, A. et al. Calcium-activated and apoptotic phospholipid scrambling induced by Ano6 can occur independently of Ano6 ion currents. Cell Death Dis. 4, e611 (2013).
    • (2013) Cell Death Dis. , vol.4 , pp. e611
    • Kmit, A.1
  • 36
    • 84872236421 scopus 로고    scopus 로고
    • Anoctamins are a family of Ca21-activated Cl2 channels
    • Tian, Y., Schreiber, R.& Kunzelmann, K. Anoctamins are a family of Ca21-activated Cl2 channels. J. Cell Sci. 125, 4991-4998 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 4991-4998
    • Tian, Y.1    Schreiber, R.2    Kunzelmann, K.3
  • 37
    • 84857129152 scopus 로고    scopus 로고
    • Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases
    • Baldridge, R. D. & Graham, T. R. Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases. Proc. Natl Acad. Sci. USA 109, E290-E298 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. E290-E298
    • Baldridge, R.D.1    Graham, T.R.2
  • 38
    • 84898045047 scopus 로고    scopus 로고
    • Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2
    • Vestergaard, A. L. et al. Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2. Proc. Natl Acad. Sci. USA 111, E1334-E1343 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E1334-E1343
    • Vestergaard, A.L.1
  • 39
    • 70349573000 scopus 로고    scopus 로고
    • TMEM16Binduces chloride currents activated by calcium in mammalian cells
    • Pifferi, S., Dibattista, M.&Menini, A.TMEM16Binduces chloride currents activated by calcium in mammalian cells. Pflugers Arch. 458, 1023-1038 (2009).
    • (2009) Pflugers Arch. , vol.458 , pp. 1023-1038
    • Pifferi, S.1    Dibattista, M.2    Menini, A.3
  • 40
    • 0015879604 scopus 로고
    • Ionic blockage of sodium channels in nerve
    • Woodhull, A. M. Ionic blockage of sodium channels in nerve. J. Gen. Physiol. 61, 687-708 (1973).
    • (1973) J. Gen. Physiol. , vol.61 , pp. 687-708
    • Woodhull, A.M.1
  • 41
    • 0029941550 scopus 로고    scopus 로고
    • Activation of calcium-dependent chloride channels in rat parotid acinar cells
    • Arreola, J., Melvin, J. E. & Begenisich, T. Activation of calcium-dependent chloride channels in rat parotid acinar cells. J. Gen. Physiol. 108, 35-47 (1996).
    • (1996) J. Gen. Physiol. , vol.108 , pp. 35-47
    • Arreola, J.1    Melvin, J.E.2    Begenisich, T.3
  • 42
    • 79957786620 scopus 로고    scopus 로고
    • Voltage-and calcium-dependent gating of TMEM16A/Ano1 chloride channels are physically coupled by the first intracellular loop
    • Xiao, Q. et al. Voltage-and calcium-dependent gating of TMEM16A/Ano1 chloride channels are physically coupled by the first intracellular loop. Proc. Natl Acad. Sci. USA 108, 8891-8896 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 8891-8896
    • Xiao, Q.1
  • 43
    • 84885454101 scopus 로고    scopus 로고
    • Calmodulin-dependent activation and inactivation of anoctamin calcium-gated chloride channels
    • Vocke, K. et al. Calmodulin-dependent activation and inactivation of anoctamin calcium-gated chloride channels. J. Gen. Physiol. 142, 381-404 (2013).
    • (2013) J. Gen. Physiol. , vol.142 , pp. 381-404
    • Vocke, K.1
  • 44
    • 84893141356 scopus 로고    scopus 로고
    • Activation of the Ano1 (TMEM16A) chloride channel by calcium is not mediated by calmodulin
    • Yu, K., Zhu, J., Qu, Z., Cui, Y. Y. & Hartzell, H. C. Activation of the Ano1 (TMEM16A) chloride channel by calcium is not mediated by calmodulin. J. Gen. Physiol. 143, 253-267 (2014).
    • (2014) J. Gen. Physiol. , vol.143 , pp. 253-267
    • Yu, K.1    Zhu, J.2    Qu, Z.3    Cui, Y.Y.4    Hartzell, H.C.5
  • 45
    • 79953863174 scopus 로고    scopus 로고
    • Calmodulin-dependent activation of the epithelial calciumdependent chloride channel TMEM16A
    • Tian, Y. et al. Calmodulin-dependent activation of the epithelial calciumdependent chloride channel TMEM16A. FASEB J. 25, 3 1058-1068 (2011).
    • (2011) FASEB J. , vol.25 , Issue.3 , pp. 1058-1068
    • Tian, Y.1
  • 46
    • 84871959313 scopus 로고    scopus 로고
    • Dynamic modulation of ANO1/TMEM16A HCO3 2 permeability by Ca21/calmodulin
    • Jung, J. et al. Dynamic modulation of ANO1/TMEM16A HCO3 2 permeability by Ca21/calmodulin. Proc. Natl Acad. Sci. USA 110, 360-365 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 360-365
    • Jung, J.1
  • 47
    • 79953845449 scopus 로고    scopus 로고
    • A versatile and efficient high-throughput cloning tool for structural biology
    • Geertsma, E. R. & Dutzler, R. A versatile and efficient high-throughput cloning tool for structural biology. Biochemistry 50, 3272-3278 (2011).
    • (2011) Biochemistry , vol.50 , pp. 3272-3278
    • Geertsma, E.R.1    Dutzler, R.2
  • 48
    • 0035543198 scopus 로고    scopus 로고
    • One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-tag
    • Keefe, A. D., Wilson, D. S., Seelig, B. & Szostak, J. W. One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-tag. Protein Expr. Purif. 23, 440-446 (2001).
    • (2001) Protein Expr. Purif. , vol.23 , pp. 440-446
    • Keefe, A.D.1    Wilson, D.S.2    Seelig, B.3    Szostak, J.W.4
  • 49
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T. et al. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nature Biotechnol. 20, 87-90 (2002).
    • (2002) Nature Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1
  • 50
    • 58849125253 scopus 로고    scopus 로고
    • A chloride conductance in VGLUT1 underlies maximal glutamate loading into synaptic vesicles
    • Schenck, S., Wojcik, S. M., Brose, N. & Takamori, S. A chloride conductance in VGLUT1 underlies maximal glutamate loading into synaptic vesicles. Nature Neurosci. 12, 156-162 (2009).
    • (2009) Nature Neurosci. , vol.12 , pp. 156-162
    • Schenck, S.1    Wojcik, S.M.2    Brose, N.3    Takamori, S.4
  • 51
    • 43149098999 scopus 로고    scopus 로고
    • GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae
    • Drew, D. et al. GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae. Nature Protocols 3, 784-798 (2008).
    • (2008) Nature Protocols , vol.3 , pp. 784-798
    • Drew, D.1
  • 52
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 53
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for X-ray crystallography
    • The Collaborative Computational Project Number 4
    • The Collaborative Computational Project, Number 4. The CCP4 suite: programs for X-ray crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 55
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for phasing with SHELX programs
    • Pape, T. & Schneider, T. R. HKL2MAP: a graphical user interface for phasing with SHELX programs. J. Appl. Crystallogr. 37, 843-844 (2004).
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 56
    • 0031059866 scopus 로고    scopus 로고
    • (eds Carter, C. W. & Sweet, R. M.) Academic
    • de La Fortelle, E.&Bricogne, G. in Methods in Enzymology Vol.276 (eds Carter, C. W. & Sweet, R. M.) 492-494 (Academic, 1997).
    • (1997) Methods in Enzymology , vol.276 , pp. 492-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 58
    • 84889120137 scopus 로고
    • Improved methods for building proteinmodels in electron densitymaps and the location of errors in thesemodels
    • Jones, T. A., Zou, J. Y., Cowan,S. W.&Kjeldgaard, M.Improved methods for building proteinmodels in electron densitymaps and the location of errors in thesemodels. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 59
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al.Phaser crystallographic software. J.Appl. Crystallogr.40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 60
    • 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
  • 61
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, 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
    • Brünger, A.T.1
  • 62
    • 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
  • 64
    • 84878651582 scopus 로고    scopus 로고
    • Functional characterization of a ClC transporter by solid-supported membrane electrophysiology
    • Garcia-Celma, J., Szydelko, A. & Dutzler, R. Functional characterization of a ClC transporter by solid-supported membrane electrophysiology. J. Gen. Physiol. 141, 479-491 (2013).
    • (2013) J. Gen. Physiol. , vol.141 , pp. 479-491
    • Garcia-Celma, J.1    Szydelko, A.2    Dutzler, R.3
  • 65
    • 0842304663 scopus 로고    scopus 로고
    • Ionic currents mediated by a prokaryotic homologue of CLC Cl2 channels
    • Accardi, A., Kolmakova-Partensky, L., Williams, C. & Miller, C. Ionic currents mediated by a prokaryotic homologue of CLC Cl2 channels. J. Gen. Physiol. 123, 109-119 (2004).
    • (2004) J. Gen. Physiol. , vol.123 , pp. 109-119
    • Accardi, A.1    Kolmakova-Partensky, L.2    Williams, C.3    Miller, C.4
  • 66
    • 79959775185 scopus 로고    scopus 로고
    • Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC
    • Zimmermann, I. & Dutzler, R. Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC. PLoS Biol. 9, e1001101 (2011).
    • (2011) PLoS Biol. , vol.9 , pp. e1001101
    • Zimmermann, I.1    Dutzler, R.2
  • 67
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality proteinmultiple sequence alignments using Clustal Omega
    • Sievers, F. et al. Fast, scalable generation of high-quality proteinmultiple sequence alignments using Clustal Omega. Mol. Syst. Biol. 7, 539 (2011).
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 539
    • Sievers, F.1


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