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Volumn 13, Issue 8, 2005, Pages 1107-1118

What makes an aquaporin a glycerol channel? A comparative study of AqpZ and GlpF

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN; AQUAPORIN Z; GLYCEROL; UNCLASSIFIED DRUG;

EID: 23044496908     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.05.005     Document Type: Article
Times cited : (149)

References (58)
  • 1
    • 11744384413 scopus 로고
    • The Grotthuss mechanism
    • N. Agmon The Grotthuss mechanism Chem. Phys. Lett. 244 1995 456 462
    • (1995) Chem. Phys. Lett. , vol.244 , pp. 456-462
    • Agmon, N.1
  • 2
    • 0032510966 scopus 로고    scopus 로고
    • The aquaporins, blueprints for cellular plumbing systems
    • P. Agre, M. Bonhivers, and M.J. Borgnia The aquaporins, blueprints for cellular plumbing systems J. Biol. Chem. 273 1998 14659 14662
    • (1998) J. Biol. Chem. , vol.273 , pp. 14659-14662
    • Agre, P.1    Bonhivers, M.2    Borgnia, M.J.3
  • 3
    • 0035956936 scopus 로고    scopus 로고
    • Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli
    • M.J. Borgnia, and P. Agre Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli Proc. Natl. Acad. Sci. USA 98 2001 2888 2893
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2888-2893
    • Borgnia, M.J.1    Agre, P.2
  • 4
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • M. Borgnia, S. Nielsen, A. Engel, and P. Agre Cellular and molecular biology of the aquaporin water channels Annu. Rev. Biochem. 68 1999 425 458
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 6
    • 33846823909 scopus 로고
    • Particle mesh Ewald. An N·log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald. An N·log(N) method for Ewald sums in large systems J. Chem. Phys. 98 1993 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 8
    • 17044406611 scopus 로고    scopus 로고
    • The dynamics and energetics of water permeation and proton exclusion in aquaporins
    • B.L. de Groot, and H. Grubmüller The dynamics and energetics of water permeation and proton exclusion in aquaporins Curr. Opin. Struct. Biol. 15 2005 1 8
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 1-8
    • De Groot, B.L.1    Grubmüller, H.2
  • 9
    • 0035979744 scopus 로고    scopus 로고
    • A refined structure of human aquaporin-1
    • B.L. de Groot, A. Engel, and H. Grubmüller A refined structure of human aquaporin-1 FEBS Lett. 504 2001 206 211
    • (2001) FEBS Lett. , vol.504 , pp. 206-211
    • De Groot, B.L.1    Engel, A.2    Grubmüller, H.3
  • 10
    • 0141534474 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in the aquaporin-1 water channel
    • B.L. de Groot, T. Frigato, V. Helms, and H. Grubmüller The mechanism of proton exclusion in the aquaporin-1 water channel J. Mol. Biol. 333 2003 279 293
    • (2003) J. Mol. Biol. , vol.333 , pp. 279-293
    • De Groot, B.L.1    Frigato, T.2    Helms, V.3    Grubmüller, H.4
  • 11
    • 0002036605 scopus 로고
    • On the decomposition of water and dissolved bodies by means of galvanic electricity
    • C.J.T. de Grotthuss On the decomposition of water and dissolved bodies by means of galvanic electricity Ann. Chim. LVIII 1806 54 74
    • (1806) Ann. Chim. , vol.58 , pp. 54-74
    • De Grotthuss, C.J.T.1
  • 12
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation - The Langevin piston method
    • S.E. Feller, Y.H. Zhang, R.W. Pastor, and B.R. Brooks Constant pressure molecular dynamics simulation - the Langevin piston method J. Chem. Phys. 103 1995 4613 4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.H.2    Pastor, R.W.3    Brooks, B.R.4
  • 14
    • 0344736695 scopus 로고    scopus 로고
    • Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates
    • M. Gao, D. Craig, O. Lequin, I.D. Campbell, V. Vogel, and K. Schulten Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates Proc. Natl. Acad. Sci. USA 100 2003 14784 14789
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14784-14789
    • Gao, M.1    Craig, D.2    Lequin, O.3    Campbell, I.D.4    Vogel, V.5    Schulten, K.6
  • 15
    • 2442659197 scopus 로고    scopus 로고
    • Aquaporin-0 membrane junctions reveal the structure of a closed water pore
    • T. Gonen, P. Sliz, J. Kistler, Y. Cheng, and T. Walz Aquaporin-0 membrane junctions reveal the structure of a closed water pore Nature 429 2004 193 197
    • (2004) Nature , vol.429 , pp. 193-197
    • Gonen, T.1    Sliz, P.2    Kistler, J.3    Cheng, Y.4    Walz, T.5
  • 16
    • 0038713404 scopus 로고    scopus 로고
    • Mechanisms of selectivity in channels and enzymes studied with interactive molecular dynamics
    • P. Grayson, E. Tajkhorshid, and K. Schulten Mechanisms of selectivity in channels and enzymes studied with interactive molecular dynamics Biophys. J. 85 2003 36 48
    • (2003) Biophys. J. , vol.85 , pp. 36-48
    • Grayson, P.1    Tajkhorshid, E.2    Schulten, K.3
  • 18
    • 0019195926 scopus 로고
    • Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli
    • K.B. Heller, E.C. Lin, and T.H. Wilson Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli J. Bacteriol. 144 1980 274 278
    • (1980) J. Bacteriol. , vol.144 , pp. 274-278
    • Heller, K.B.1    Lin, E.C.2    Wilson, T.H.3
  • 19
    • 0033446707 scopus 로고    scopus 로고
    • Aquaporins: Phylogeny, structure, and physiology of water channels
    • J.B. Heynmann, and A. Engel Aquaporins: phylogeny, structure, and physiology of water channels News Physiol. Sci. 14 1999 187 193
    • (1999) News Physiol. Sci. , vol.14 , pp. 187-193
    • Heynmann, J.B.1    Engel, A.2
  • 20
    • 0035829539 scopus 로고    scopus 로고
    • Water conduction through the hydrophobic channel of a carbon nanotube
    • G. Hummer, J.C. Rasaiah, and J.P. Noworyta Water conduction through the hydrophobic channel of a carbon nanotube Nature 414 2001 188 190
    • (2001) Nature , vol.414 , pp. 188-190
    • Hummer, G.1    Rasaiah, J.C.2    Noworyta, J.P.3
  • 22
    • 0037131175 scopus 로고    scopus 로고
    • Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63
    • M. Ikeda, E. Beitz, D. Kozono, W.B. Guggino, P. Agre, and M. Yasui Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63 J. Biol. Chem. 277 2002 39873 39879
    • (2002) J. Biol. Chem. , vol.277 , pp. 39873-39879
    • Ikeda, M.1    Beitz, E.2    Kozono, D.3    Guggino, W.B.4    Agre, P.5    Yasui, M.6
  • 23
    • 1842583051 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in aquaporin channels
    • B. Ilan, E. Tajkhorshid, K. Schulten, and G.A. Voth The mechanism of proton exclusion in aquaporin channels Proteins 55 2004 223 228
    • (2004) Proteins , vol.55 , pp. 223-228
    • Ilan, B.1    Tajkhorshid, E.2    Schulten, K.3    Voth, G.A.4
  • 25
    • 4244116139 scopus 로고    scopus 로고
    • Equilibrium free-energy differences from nonequilibrium measurements: A master equation approach
    • C. Jarzynski Equilibrium free-energy differences from nonequilibrium measurements: a master equation approach Phys. Rev. E 56 1997 5018 5035
    • (1997) Phys. Rev. e , vol.56 , pp. 5018-5035
    • Jarzynski, C.1
  • 26
    • 4243754128 scopus 로고    scopus 로고
    • Nonequilibrium equality for free energy differences
    • C. Jarzynski Nonequilibrium equality for free energy differences Phys. Rev. Lett. 78 1997 2690 2693
    • (1997) Phys. Rev. Lett. , vol.78 , pp. 2690-2693
    • Jarzynski, C.1
  • 27
    • 0035183282 scopus 로고    scopus 로고
    • The mechanism of glycerol conduction in aquaglyceroporins
    • M.Ø. Jensen, E. Tajkhorshid, and K. Schulten The mechanism of glycerol conduction in aquaglyceroporins Structure 9 2001 1083 1093
    • (2001) Structure , vol.9 , pp. 1083-1093
    • Jensen M.Ø1    Tajkhorshid, E.2    Schulten, K.3
  • 29
    • 0242269040 scopus 로고    scopus 로고
    • Electrostatic tuning of permeation and selectivity in aquaporin water channels
    • M.Ø. Jensen, E. Tajkhorshid, and K. Schulten Electrostatic tuning of permeation and selectivity in aquaporin water channels Biophys. J. 85 2003 2884 2899
    • (2003) Biophys. J. , vol.85 , pp. 2884-2899
    • Jensen M.Ø1    Tajkhorshid, E.2    Schulten, K.3
  • 31
    • 0035903098 scopus 로고    scopus 로고
    • Impaired hearing in mice lacking aquaporin-4 water channels
    • J. Li, and A.S. Verkman Impaired hearing in mice lacking aquaporin-4 water channels J. Biol. Chem. 276 2001 31233 31237
    • (2001) J. Biol. Chem. , vol.276 , pp. 31233-31237
    • Li, J.1    Verkman, A.S.2
  • 33
    • 0033917135 scopus 로고    scopus 로고
    • The key event in force-induced unfolding of titin's immunoglobulin domains
    • H. Lu, and K. Schulten The key event in force-induced unfolding of titin's immunoglobulin domains Biophys. J. 79 2000 51 65
    • (2000) Biophys. J. , vol.79 , pp. 51-65
    • Lu, H.1    Schulten, K.2
  • 34
    • 0242332305 scopus 로고    scopus 로고
    • Glycerol conductance and physical asymmetry of the Escherichia coli glycerol facilitator GlpF
    • D. Lu, P. Grayson, and K. Schulten Glycerol conductance and physical asymmetry of the Escherichia coli glycerol facilitator GlpF Biophys. J. 85 2003 2977 2987
    • (2003) Biophys. J. , vol.85 , pp. 2977-2987
    • Lu, D.1    Grayson, P.2    Schulten, K.3
  • 37
    • 0345613372 scopus 로고
    • Molecular mechanisms for proton transport in membranes
    • J.F. Nagle, and H.J. Morowitz Molecular mechanisms for proton transport in membranes Proc. Natl. Acad. Sci. USA 75 1978 298 302
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 298-302
    • Nagle, J.F.1    Morowitz, H.J.2
  • 38
    • 13844266306 scopus 로고    scopus 로고
    • Evolutionary profiles derived from the QR factorization of multiple structural alignments gives an economy of information
    • P. O'Donoghue, and Z. Luthey-Schulten Evolutionary profiles derived from the QR factorization of multiple structural alignments gives an economy of information J. Mol. Biol. 346 2005 875 894
    • (2005) J. Mol. Biol. , vol.346 , pp. 875-894
    • O'Donoghue, P.1    Luthey-Schulten, Z.2
  • 39
    • 4143087050 scopus 로고    scopus 로고
    • Calculating potentials of mean force from steered molecular dynamics simulations
    • S. Park, and K. Schulten Calculating potentials of mean force from steered molecular dynamics simulations J. Chem. Phys. 120 2004 5946 5961
    • (2004) J. Chem. Phys. , vol.120 , pp. 5946-5961
    • Park, S.1    Schulten, K.2
  • 40
    • 0042885340 scopus 로고    scopus 로고
    • Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality
    • S. Park, F. Khalili-Araghi, E. Tajkhorshid, and K. Schulten Free energy calculation from steered molecular dynamics simulations using Jarzynski's equality J. Chem. Phys. 119 2003 3559 3566
    • (2003) J. Chem. Phys. , vol.119 , pp. 3559-3566
    • Park, S.1    Khalili-Araghi, F.2    Tajkhorshid, E.3    Schulten, K.4
  • 41
    • 0030011088 scopus 로고    scopus 로고
    • + translocation along the single-file water chain in the gramicidin a channel
    • + translocation along the single-file water chain in the gramicidin A channel Biophys. J. 71 1996 19 39
    • (1996) Biophys. J. , vol.71 , pp. 19-39
    • Pomès, R.1    Roux, B.2
  • 42
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • G.M. Preston, T.P. Carroll, W.B. Guggino, and P. Agre Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein Science 256 1992 385 387
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 43
    • 4143116650 scopus 로고    scopus 로고
    • Computational studies of membrane channels
    • B. Roux, and K. Schulten Computational studies of membrane channels Structure 12 2004 1343 1351
    • (2004) Structure , vol.12 , pp. 1343-1351
    • Roux, B.1    Schulten, K.2
  • 44
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • R.B. Russell, and G. Barton Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels Proteins 14 1992 309 323
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.2
  • 45
    • 0035936571 scopus 로고    scopus 로고
    • Membrane proteins: Aquaporins - Channels without ions
    • M.S.P. Sansom, and R.J. Law Membrane proteins: aquaporins - channels without ions Curr. Biol. 11 2001 R71 R73
    • (2001) Curr. Biol. , vol.11
    • Sansom, M.S.P.1    Law, R.J.2
  • 48
    • 0022520349 scopus 로고
    • Proton conduction through proteins: An overview of theoretical principles and applications
    • Z. Schulten, and K. Schulten Proton conduction through proteins: an overview of theoretical principles and applications Methods Enzymol. 127 1986 419 438
    • (1986) Methods Enzymol. , vol.127 , pp. 419-438
    • Schulten, Z.1    Schulten, K.2
  • 49
    • 0027145628 scopus 로고
    • The pore dimensions of gramicidin a
    • O. Smart, J. Goodfellow, and B. Wallace The pore dimensions of gramicidin A Biophys. J. 65 1993 2455 2460
    • (1993) Biophys. J. , vol.65 , pp. 2455-2460
    • Smart, O.1    Goodfellow, J.2    Wallace, B.3
  • 50
    • 17044401714 scopus 로고    scopus 로고
    • In search of the hair-cell gating spring: Elastic properties of ankyrin and cadherin repeats
    • M. Sotomayor, D.P. Corey, and K. Schulten In search of the hair-cell gating spring: elastic properties of ankyrin and cadherin repeats Structure 13 2005 669 682
    • (2005) Structure , vol.13 , pp. 669-682
    • Sotomayor, M.1    Corey, D.P.2    Schulten, K.3
  • 51
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • H. Sui, B.-G. Han, J.K. Lee, P. Walian, and B.K. Jap Structural basis of water-specific transport through the AQP1 water channel Nature 414 2001 872 878
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.-G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 54
    • 0036544847 scopus 로고    scopus 로고
    • New roles for old holes: Ion channel function in aquaporin-1
    • A.J. Yool, and A.M. Weinstein New roles for old holes: ion channel function in aquaporin-1 News Physiol. Sci. 17 2002 68 72
    • (2002) News Physiol. Sci. , vol.17 , pp. 68-72
    • Yool, A.J.1    Weinstein, A.M.2
  • 55
    • 0037861907 scopus 로고    scopus 로고
    • Water and proton conduction through carbon nanotubes as models for biological channels
    • F. Zhu, and K. Schulten Water and proton conduction through carbon nanotubes as models for biological channels Biophys. J. 85 2003 236 244
    • (2003) Biophys. J. , vol.85 , pp. 236-244
    • Zhu, F.1    Schulten, K.2
  • 56
    • 0035979666 scopus 로고    scopus 로고
    • Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer
    • F. Zhu, E. Tajkhorshid, and K. Schulten Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer FEBS Lett. 504 2001 212 218
    • (2001) FEBS Lett. , vol.504 , pp. 212-218
    • Zhu, F.1    Tajkhorshid, E.2    Schulten, K.3
  • 57
    • 42749105522 scopus 로고    scopus 로고
    • Collective diffusion model for water permeation through microscopic channels
    • F. Zhu, E. Tajkhorshid, and K. Schulten Collective diffusion model for water permeation through microscopic channels Phys. Rev. Lett. 93 2004 224501
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 224501
    • Zhu, F.1    Tajkhorshid, E.2    Schulten, K.3
  • 58
    • 22844455879 scopus 로고    scopus 로고
    • Hydrogen bonds with large proton polarizability and proton transfer processes in electrochemistry and biology
    • G. Zundel Hydrogen bonds with large proton polarizability and proton transfer processes in electrochemistry and biology Adv. Chem. Phys. 111 2000 1 217
    • (2000) Adv. Chem. Phys. , vol.111 , pp. 1-217
    • Zundel, G.1


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