메뉴 건너뛰기




Volumn 22, Issue 11, 2014, Pages 1677-1686

Determining the oligomeric structure of proteorhodopsin by gd3+-based pulsed dipolar spectroscopy of multiple distances

Author keywords

[No Author keywords available]

Indexed keywords

GADOLINIUM; MEMBRANE PROTEIN; NITROXIDE; OLIGOMER; RHODOPSIN; THREONINE; TRYPSIN; NITROGEN OXIDE; PROTEORHODOPSIN; SPIN LABELING;

EID: 84908512395     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.09.008     Document Type: Article
Times cited : (71)

References (73)
  • 1
    • 44949236117 scopus 로고    scopus 로고
    • High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation
    • C. Altenbach, A.K. Kusnetzow, O.P. Ernst, K.P. Hofmann, and W.L. Hubbell High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation Proc. Natl. Acad. Sci. USA 105 2008 7439 7444
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7439-7444
    • Altenbach, C.1    Kusnetzow, A.K.2    Ernst, O.P.3    Hofmann, K.P.4    Hubbell, W.L.5
  • 10
    • 84869394927 scopus 로고    scopus 로고
    • Oligomerization of polytopic α-helical membrane proteins: Causes and consequences
    • F. Cymer, and D. Schneider Oligomerization of polytopic α-helical membrane proteins: causes and consequences Biol. Chem. 393 2012 1215 1230
    • (2012) Biol. Chem. , vol.393 , pp. 1215-1230
    • Cymer, F.1    Schneider, D.2
  • 11
    • 84867053372 scopus 로고    scopus 로고
    • Symmetry-constrained analysis of pulsed double electron-electron resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate
    • O. Dalmas, H.C. Hyde, R.E. Hulse, and E. Perozo Symmetry-constrained analysis of pulsed double electron-electron resonance (DEER) spectroscopy reveals the dynamic nature of the KcsA activation gate J. Am. Chem. Soc. 134 2012 16360 16369
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16360-16369
    • Dalmas, O.1    Hyde, H.C.2    Hulse, R.E.3    Perozo, E.4
  • 12
    • 77951701764 scopus 로고    scopus 로고
    • The light-driven proton pump proteorhodopsin enhances bacterial survival during tough times
    • E.F. DeLong, and O. Béjà The light-driven proton pump proteorhodopsin enhances bacterial survival during tough times PLoS Biol. 8 2010 e1000359
    • (2010) PLoS Biol. , vol.8 , pp. 1000359
    • Delong, E.F.1    Béjà, O.2
  • 13
    • 0038390509 scopus 로고    scopus 로고
    • Proton transport by proteorhodopsin requires that the retinal Schiff base counterion Asp-97 be anionic
    • A.K. Dioumaev, J.M. Wang, Z. Bálint, G. Váró, and J.K. Lanyi Proton transport by proteorhodopsin requires that the retinal Schiff base counterion Asp-97 be anionic Biochemistry 42 2003 6582 6587
    • (2003) Biochemistry , vol.42 , pp. 6582-6587
    • Dioumaev, A.K.1    Wang, J.M.2    Bálint, Z.3    Váró, G.4    Lanyi, J.K.5
  • 14
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • L. Essen, R. Siegert, W.D. Lehmann, and D. Oesterhelt Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex Proc. Natl. Acad. Sci. USA 95 1998 11673 11678
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 15
    • 72449211146 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled receptors: A reality
    • S. Ferré, and R. Franco Oligomerization of G-protein-coupled receptors: a reality Curr. Opin. Pharmacol. 10 2010 1 5
    • (2010) Curr. Opin. Pharmacol. , vol.10 , pp. 1-5
    • Ferré, S.1    Franco, R.2
  • 21
    • 84899850617 scopus 로고    scopus 로고
    • Gd3+ spin labeling for distance measurements by pulse EPR spectroscopy
    • D. Goldfarb Gd3+ spin labeling for distance measurements by pulse EPR spectroscopy Phys. Chem. Chem. Phys. 16 2014 9685 9699
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 9685-9699
    • Goldfarb, D.1
  • 23
    • 79957516738 scopus 로고    scopus 로고
    • GPCR oligomers in pharmacology and signaling
    • J. González-Maeso GPCR oligomers in pharmacology and signaling Mol. Brain 4 2011 20
    • (2011) Mol. Brain , vol.4 , pp. 20
    • González-Maeso, J.1
  • 24
    • 79959731607 scopus 로고    scopus 로고
    • W-Band pulse EPR distance measurements in peptides using Gd(3+)-dipicolinic acid derivatives as spin labels
    • M. Gordon-Grossman, I. Kaminker, Y. Gofman, Y. Shai, and D. Goldfarb W-Band pulse EPR distance measurements in peptides using Gd(3+)-dipicolinic acid derivatives as spin labels Phys. Chem. Chem. Phys. 13 2011 10771 10780
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 10771-10780
    • Gordon-Grossman, M.1    Kaminker, I.2    Gofman, Y.3    Shai, Y.4    Goldfarb, D.5
  • 27
    • 23244454211 scopus 로고    scopus 로고
    • Assessing oligomerization of membrane proteins by four-pulse DEER: PH-dependent dimerization of NhaA Na+/H+ antiporter of E.coli
    • D. Hilger, H. Jung, E. Padan, C. Wegener, K.-P. Vogel, H.-J. Steinhoff, and G. Jeschke Assessing oligomerization of membrane proteins by four-pulse DEER: pH-dependent dimerization of NhaA Na+/H+ antiporter of E. coli Biophys. J. 89 2005 1328 1338
    • (2005) Biophys. J. , vol.89 , pp. 1328-1338
    • Hilger, D.1    Jung, H.2    Padan, E.3    Wegener, C.4    Vogel, K.-P.5    Steinhoff, H.-J.6    Jeschke, G.7
  • 29
    • 77950283310 scopus 로고    scopus 로고
    • Studying the stoichiometries of membrane proteins by mass spectrometry: Microbial rhodopsins and a potassium ion channel
    • J. Hoffmann, L. Aslimovska, C. Bamann, C. Glaubitz, E. Bamberg, and B. Brutschy Studying the stoichiometries of membrane proteins by mass spectrometry: microbial rhodopsins and a potassium ion channel Phys. Chem. Chem. Phys. 12 2010 3480 3485
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 3480-3485
    • Hoffmann, J.1    Aslimovska, L.2    Bamann, C.3    Glaubitz, C.4    Bamberg, E.5    Brutschy, B.6
  • 30
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • W.L. Hubbell, D.S. Cafiso, and C. Altenbach Identifying conformational changes with site-directed spin labeling Nat. Struct. Biol. 7 2000 735 739
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 32
    • 84873535860 scopus 로고    scopus 로고
    • Transmembrane protein activation refined by site-specific hydration dynamics
    • S. Hussain, J.M. Franck, and S. Han Transmembrane protein activation refined by site-specific hydration dynamics Angew. Chem. Int. Ed. Engl. 52 2013 1953 1958
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 1953-1958
    • Hussain, S.1    Franck, J.M.2    Han, S.3
  • 33
    • 0036004918 scopus 로고    scopus 로고
    • Determination of the nanostructure of polymer materials by electron paramagnetic resonance spectroscopy
    • G. Jeschke Determination of the nanostructure of polymer materials by electron paramagnetic resonance spectroscopy Macromol. Rapid Commun. 23 2002 227 246
    • (2002) Macromol. Rapid Commun. , vol.23 , pp. 227-246
    • Jeschke, G.1
  • 34
    • 84877303485 scopus 로고    scopus 로고
    • A comparative study of structures and structural transitions of secondary transporters with the LeuT fold
    • G. Jeschke A comparative study of structures and structural transitions of secondary transporters with the LeuT fold Eur. Biophys. J. 42 2013 181 197
    • (2013) Eur. Biophys. J. , vol.42 , pp. 181-197
    • Jeschke, G.1
  • 36
    • 34147218123 scopus 로고    scopus 로고
    • Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance
    • G. Jeschke, and Y. Polyhach Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance Phys. Chem. Chem. Phys. 9 2007 1895 1910
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 1895-1910
    • Jeschke, G.1    Polyhach, Y.2
  • 38
    • 68349085642 scopus 로고    scopus 로고
    • Three-spin correlations in double electron-electron resonance
    • G. Jeschke, M. Sajid, M. Schulte, and A. Godt Three-spin correlations in double electron-electron resonance Phys. Chem. Chem. Phys. 11 2009 6580 6591
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 6580-6591
    • Jeschke, G.1    Sajid, M.2    Schulte, M.3    Godt, A.4
  • 39
    • 78149437446 scopus 로고    scopus 로고
    • The distribution of fatty acids reveals the functional structure of human serum albumin
    • M.J.N. Junk, H.W. Spiess, and D. Hinderberger The distribution of fatty acids reveals the functional structure of human serum albumin Angew. Chem. Int. Ed. Engl. 49 2010 8755 8759
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 8755-8759
    • Junk, M.J.N.1    Spiess, H.W.2    Hinderberger, D.3
  • 40
    • 79955925395 scopus 로고    scopus 로고
    • DEER in biological multispin-systems: A case study on the fatty acid binding to human serum albumin
    • M.J.N. Junk, H.W. Spiess, and D. Hinderberger DEER in biological multispin-systems: a case study on the fatty acid binding to human serum albumin J. Magn. Reson. 210 2011 210 217
    • (2011) J. Magn. Reson. , vol.210 , pp. 210-217
    • Junk, M.J.N.1    Spiess, H.W.2    Hinderberger, D.3
  • 41
    • 84858402344 scopus 로고    scopus 로고
    • Spectroscopic selection of distance measurements in a protein dimer with mixed nitroxide and Gd3+ spin labels
    • I. Kaminker, H. Yagi, T. Huber, A. Feintuch, G. Otting, and D. Goldfarb Spectroscopic selection of distance measurements in a protein dimer with mixed nitroxide and Gd3+ spin labels Phys. Chem. Chem. Phys. 14 2012 4355 4358
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 4355-4358
    • Kaminker, I.1    Yagi, H.2    Huber, T.3    Feintuch, A.4    Otting, G.5    Goldfarb, D.6
  • 43
    • 34248337035 scopus 로고    scopus 로고
    • Detection of fast light-activated H+ release and M intermediate formation from proteorhodopsin
    • R.A. Krebs, U. Alexiev, R. Partha, A.M. DeVita, and M.S. Braiman Detection of fast light-activated H+ release and M intermediate formation from proteorhodopsin BMC Physiol. 2 2002 5
    • (2002) BMC Physiol. , vol.2 , pp. 5
    • Krebs, R.A.1    Alexiev, U.2    Partha, R.3    Devita, A.M.4    Braiman, M.S.5
  • 45
    • 70349554681 scopus 로고    scopus 로고
    • Voltage- and pH-dependent changes in vectoriality of photocurrents mediated by wild-type and mutant proteorhodopsins upon expression in Xenopus oocytes
    • E. Lörinczi, M.-K. Verhoefen, J. Wachtveitl, A.C. Woerner, C. Glaubitz, M. Engelhard, E. Bamberg, and T. Friedrich Voltage- and pH-dependent changes in vectoriality of photocurrents mediated by wild-type and mutant proteorhodopsins upon expression in Xenopus oocytes J. Mol. Biol. 393 2009 320 341
    • (2009) J. Mol. Biol. , vol.393 , pp. 320-341
    • Lörinczi, E.1    Verhoefen, M.-K.2    Wachtveitl, J.3    Woerner, A.C.4    Glaubitz, C.5    Engelhard, M.6    Bamberg, E.7    Friedrich, T.8
  • 46
    • 79952787086 scopus 로고    scopus 로고
    • Double Electron-Electron Resonance Measured between Gd3+ Ions and Nitroxide Radicals
    • P. Lueders, G. Jeschke, and M. Yulikov Double Electron-Electron Resonance Measured Between Gd3+ Ions and Nitroxide Radicals J. Phys. Chem. Lett. 2 2011 604 609
    • (2011) J. Phys. Chem. Lett. , vol.2 , pp. 604-609
    • Lueders, P.1    Jeschke, G.2    Yulikov, M.3
  • 47
    • 45449105164 scopus 로고    scopus 로고
    • Protein modulation of lipids, and vice-versa, in membranes
    • D. Marsh Protein modulation of lipids, and vice-versa, in membranes Biochim. Biophys. Acta 1778 2008 1545 1575
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1545-1575
    • Marsh, D.1
  • 49
    • 84874627264 scopus 로고    scopus 로고
    • Topology of the trans-membrane peptide WALP23 in model membranes under negative mismatch conditions
    • E. Matalon, I. Kaminker, H. Zimmermann, M. Eisenstein, Y. Shai, and D. Goldfarb Topology of the trans-membrane peptide WALP23 in model membranes under negative mismatch conditions J. Phys. Chem. B 117 2013 2280 2293
    • (2013) J. Phys. Chem. B , vol.117 , pp. 2280-2293
    • Matalon, E.1    Kaminker, I.2    Zimmermann, H.3    Eisenstein, M.4    Shai, Y.5    Goldfarb, D.6
  • 50
    • 80855144806 scopus 로고    scopus 로고
    • Toward the fourth dimension of membrane protein structure: Insight into dynamics from spin-labeling EPR spectroscopy
    • H.S. McHaourab, P.R. Steed, and K. Kazmier Toward the fourth dimension of membrane protein structure: insight into dynamics from spin-labeling EPR spectroscopy Structure 19 2011 1549 1561
    • (2011) Structure , vol.19 , pp. 1549-1561
    • McHaourab, H.S.1    Steed, P.R.2    Kazmier, K.3
  • 51
    • 0000330099 scopus 로고
    • Application of the double resonance method to electron spin echo in a study of the spatial distribution of paramagnetic centers in solids
    • A. Milov, K. Salikhov, and M. Shirov Application of the double resonance method to electron spin echo in a study of the spatial distribution of paramagnetic centers in solids Sov. Phys. Solid State 23 1981 565 569
    • (1981) Sov. Phys. Solid State , vol.23 , pp. 565-569
    • Milov, A.1    Salikhov, K.2    Shirov, M.3
  • 52
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • M. Pannier, S. Veit, A. Godt, G. Jeschke, and H.W. Spiess Dead-time free measurement of dipole-dipole interactions between electron spins J. Magn. Reson. 142 2000 331 340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 53
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • R. Phillips, T. Ursell, P. Wiggins, and P. Sens Emerging roles for lipids in shaping membrane-protein function Nature 459 2009 379 385
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 55
    • 33947620119 scopus 로고    scopus 로고
    • Spin pair geometry revealed by high-field DEER in the presence of conformational distributions
    • Y. Polyhach, A. Godt, C. Bauer, and G. Jeschke Spin pair geometry revealed by high-field DEER in the presence of conformational distributions J. Magn. Reson. 185 2007 118 129
    • (2007) J. Magn. Reson. , vol.185 , pp. 118-129
    • Polyhach, Y.1    Godt, A.2    Bauer, C.3    Jeschke, G.4
  • 56
    • 77954273484 scopus 로고    scopus 로고
    • Distance measurements in model bis-Gd(III) complexes with flexible "bridge". Emulation of biological molecules having flexible structure with Gd(III) labels attached
    • A. Potapov, Y. Song, T.J. Meade, D. Goldfarb, A.V. Astashkin, and A. Raitsimring Distance measurements in model bis-Gd(III) complexes with flexible "bridge". Emulation of biological molecules having flexible structure with Gd(III) labels attached J. Magn. Reson. 205 2010 38 49
    • (2010) J. Magn. Reson. , vol.205 , pp. 38-49
    • Potapov, A.1    Song, Y.2    Meade, T.J.3    Goldfarb, D.4    Astashkin, A.V.5    Raitsimring, A.6
  • 59
    • 84877599163 scopus 로고    scopus 로고
    • Optimization of pulsed DEER measurements for Gd-based labels: Choice of operational frequencies, pulse durations and positions, and temperature
    • A. Raitsimring, A.V. Astashkin, J.H. Enemark, I. Kaminker, D. Goldfarb, E.D. Walter, Y. Song, and T.J. Meade Optimization of pulsed DEER measurements for Gd-based labels: choice of operational frequencies, pulse durations and positions, and temperature Appl. Magn. Reson. 44 2013 649 670
    • (2013) Appl. Magn. Reson. , vol.44 , pp. 649-670
    • Raitsimring, A.1    Astashkin, A.V.2    Enemark, J.H.3    Kaminker, I.4    Goldfarb, D.5    Walter, E.D.6    Song, Y.7    Meade, T.J.8
  • 63
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Šali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Šali, A.1    Blundell, T.L.2
  • 66
    • 79955059401 scopus 로고    scopus 로고
    • Pulsed dipolar spectroscopy distance measurements in biomacromolecules labeled with Gd(III) markers
    • Y. Song, T.J. Meade, A.V. Astashkin, E.L. Klein, J.H. Enemark, and A. Raitsimring Pulsed dipolar spectroscopy distance measurements in biomacromolecules labeled with Gd(III) markers J. Magn. Reson. 210 2011 59 68
    • (2011) J. Magn. Reson. , vol.210 , pp. 59-68
    • Song, Y.1    Meade, T.J.2    Astashkin, A.V.3    Klein, E.L.4    Enemark, J.H.5    Raitsimring, A.6
  • 69
    • 84876516152 scopus 로고    scopus 로고
    • Suppression of ghost distances in multiple-spin double electron-electron resonance
    • T. von Hagens, Y. Polyhach, M. Sajid, A. Godt, and G. Jeschke Suppression of ghost distances in multiple-spin double electron-electron resonance Phys. Chem. Chem. Phys. 15 2013 5854 5866
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 5854-5866
    • Von Hagens, T.1    Polyhach, Y.2    Sajid, M.3    Godt, A.4    Jeschke, G.5
  • 70
    • 0141817991 scopus 로고    scopus 로고
    • Spectroscopic and photochemical characterization of a deep ocean proteorhodopsin
    • W.-W. Wang, O.A. Sineshchekov, E.N. Spudich, and J.L. Spudich Spectroscopic and photochemical characterization of a deep ocean proteorhodopsin J. Biol. Chem. 278 2003 33985 33991
    • (2003) J. Biol. Chem. , vol.278 , pp. 33985-33991
    • Wang, W.-W.1    Sineshchekov, O.A.2    Spudich, E.N.3    Spudich, J.L.4
  • 72
    • 79960059173 scopus 로고    scopus 로고
    • Gadolinium tagging for high-precision measurements of 6 nm distances in protein assemblies by EPR
    • H. Yagi, D. Banerjee, B. Graham, T. Huber, D. Goldfarb, and G. Otting Gadolinium tagging for high-precision measurements of 6 nm distances in protein assemblies by EPR J. Am. Chem. Soc. 133 2011 10418 10421
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 10418-10421
    • Yagi, H.1    Banerjee, D.2    Graham, B.3    Huber, T.4    Goldfarb, D.5    Otting, G.6
  • 73
    • 84863959223 scopus 로고    scopus 로고
    • Distance measurements in Au nanoparticles functionalized with nitroxide radicals and Gd(3+)-DTPA chelate complexes
    • M. Yulikov, P. Lueders, M.F. Warsi, V. Chechik, and G. Jeschke Distance measurements in Au nanoparticles functionalized with nitroxide radicals and Gd(3+)-DTPA chelate complexes Phys. Chem. Chem. Phys. 14 2012 10732 10746
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 10732-10746
    • Yulikov, M.1    Lueders, P.2    Warsi, M.F.3    Chechik, V.4    Jeschke, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.