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Volumn 113, Issue 44, 2016, Pages 12420-12425

Crystal structure of a LacY-nanobody complex in a periplasmic-open conformation

Author keywords

Bioenergetics; Fluorescence; Kinetics; Membrane transporter; X ray structure

Indexed keywords

ESCHERICHIA COLI PROTEIN; GALACTOSIDE; LACTOSE PERMEASE; LACTOSE PERMEASE LACY; MUTANT PROTEIN; NANOBODY; SUGAR; UNCLASSIFIED DRUG; COTRANSPORTER; GLUCOSE TRANSPORTER; LACY PROTEIN, E COLI; PROTEIN BINDING;

EID: 84994553250     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1615414113     Document Type: Article
Times cited : (35)

References (42)
  • 3
    • 84922214883 scopus 로고    scopus 로고
    • A chemiosmotic mechanism of symport
    • Kaback HR (2015) A chemiosmotic mechanism of symport. Proc Natl Acad Sci USA 112(5): 1259-1264.
    • (2015) Proc Natl Acad Sci USA , vol.112 , Issue.5 , pp. 1259-1264
    • Kaback, H.R.1
  • 4
    • 0017342875 scopus 로고
    • The electrochemical proton gradient in Escherichia coli membrane vesicles
    • Ramos S, Kaback HR (1977) The electrochemical proton gradient in Escherichia coli membrane vesicles. Biochemistry 16(5): 848-854.
    • (1977) Biochemistry , vol.16 , Issue.5 , pp. 848-854
    • Ramos, S.1    Kaback, H.R.2
  • 5
    • 0017616591 scopus 로고
    • The relationship between the electrochemical proton gradient and active transport in Escherichia coli membrane vesicles
    • Ramos S, Kaback HR (1977) The relationship between the electrochemical proton gradient and active transport in Escherichia coli membrane vesicles. Biochemistry 16(5): 854-859.
    • (1977) Biochemistry , vol.16 , Issue.5 , pp. 854-859
    • Ramos, S.1    Kaback, H.R.2
  • 6
    • 0018626568 scopus 로고
    • Mechanism of lactose translocation in membrane vesicles from Escherichia coli. 2. Effect of imposed Delta psi
    • Kaczorowski GJ, Robertson DE, Kaback HR (1979) Mechanism of lactose translocation in membrane vesicles from Escherichia coli. 2. Effect of imposed Delta psi, Delta pH, and Delta mu H+. Biochemistry 18(17): 3697-3704.
    • (1979) Delta pH, and Delta mu H+. Biochemistry , vol.18 , Issue.17 , pp. 3697-3704
    • Kaczorowski, G.J.1    Robertson, D.E.2    Kaback, H.R.3
  • 7
    • 0019297953 scopus 로고
    • Active transport in membrane vesicles from Escherichia coli: The electrochemical proton gradient alters the distribution of the lac carrier between two different kinetic states
    • Robertson DE, Kaczorowski GJ, Garcia ML, Kaback HR (1980) Active transport in membrane vesicles from Escherichia coli: The electrochemical proton gradient alters the distribution of the lac carrier between two different kinetic states. Biochemistry 19(25): 5692-5702.
    • (1980) Biochemistry , vol.19 , Issue.25 , pp. 5692-5702
    • Robertson, D.E.1    Kaczorowski, G.J.2    Garcia, M.L.3    Kaback, H.R.4
  • 8
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson J, et al. (2003) Structure and mechanism of the lactose permease of Escherichia coli. Science 301(5633): 610-615.
    • (2003) Science , vol.301 , Issue.5633 , pp. 610-615
    • Abramson, J.1
  • 9
    • 33645320817 scopus 로고    scopus 로고
    • Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY
    • Mirza O, Guan L, Verner G, Iwata S, Kaback HR (2006) Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY. EMBO J 25(6): 1177-1183.
    • (2006) EMBO J , vol.25 , Issue.6 , pp. 1177-1183
    • Mirza, O.1    Guan, L.2    Verner, G.3    Iwata, S.4    Kaback, H.R.5
  • 10
    • 79959349280 scopus 로고    scopus 로고
    • Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition
    • Chaptal V, et al. (2011) Crystal structure of lactose permease in complex with an affinity inactivator yields unique insight into sugar recognition. Proc Natl Acad Sci USA 108(23): 9361-9366.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.23 , pp. 9361-9366
    • Chaptal, V.1
  • 12
    • 34547880034 scopus 로고    scopus 로고
    • Single-molecule FRET reveals sugar-induced conformational dynamics in LacY
    • Majumdar DS, et al. (2007) Single-molecule FRET reveals sugar-induced conformational dynamics in LacY. Proc Natl Acad Sci USA 104(31): 12640-12645.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.31 , pp. 12640-12645
    • Majumdar, D.S.1
  • 13
    • 33846277908 scopus 로고    scopus 로고
    • Site-directed alkylation and the alternating access model for LacY
    • Kaback HR, et al. (2007) Site-directed alkylation and the alternating access model for LacY. Proc Natl Acad Sci USA 104(2): 491-494.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.2 , pp. 491-494
    • Kaback, H.R.1
  • 14
    • 36749074450 scopus 로고    scopus 로고
    • Sugar binding induces an outward facing conformation of LacY
    • Smirnova I, et al. (2007) Sugar binding induces an outward facing conformation of LacY. Proc Natl Acad Sci USA 104(42): 16504-16509.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.42 , pp. 16504-16509
    • Smirnova, I.1
  • 15
    • 41649112580 scopus 로고    scopus 로고
    • Opening and closing of the periplasmic gate in lactose permease
    • Zhou Y, Guan L, Freites JA, Kaback HR (2008) Opening and closing of the periplasmic gate in lactose permease. Proc Natl Acad Sci USA 105(10): 3774-3778.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.10 , pp. 3774-3778
    • Zhou, Y.1    Guan, L.2    Freites, J.A.3    Kaback, H.R.4
  • 16
    • 77953101915 scopus 로고    scopus 로고
    • Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane
    • Nie Y, Kaback HR (2010) Sugar binding induces the same global conformational change in purified LacY as in the native bacterial membrane. Proc Natl Acad Sci USA 107(21): 9903-9908.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.21 , pp. 9903-9908
    • Nie, Y.1    Kaback, H.R.2
  • 17
    • 84878464140 scopus 로고    scopus 로고
    • Trp replacements for tightly interacting Gly-Gly pairs in LacY stabilize an outward-facing conformation
    • Smirnova I, Kasho V, Sugihara J, Kaback HR (2013) Trp replacements for tightly interacting Gly-Gly pairs in LacY stabilize an outward-facing conformation. Proc Natl Acad Sci USA 110(22): 8876-8881.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.22 , pp. 8876-8881
    • Smirnova, I.1    Kasho, V.2    Sugihara, J.3    Kaback, H.R.4
  • 18
    • 84893445590 scopus 로고    scopus 로고
    • Structure of sugar-bound LacY
    • Kumar H, et al. (2014) Structure of sugar-bound LacY. Proc Natl Acad Sci USA 111(5): 1784-1788.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.5 , pp. 1784-1788
    • Kumar, H.1
  • 19
    • 84937697341 scopus 로고    scopus 로고
    • Structure of LacY with an a-substituted galactoside: Connecting the binding site to the protonation site
    • Kumar H, Finer-Moore JS, Kaback HR, Stroud RM (2015) Structure of LacY with an a-substituted galactoside: Connecting the binding site to the protonation site. Proc Natl Acad Sci USA 112(29): 9004-9009.
    • (2015) Proc Natl Acad Sci USA , vol.112 , Issue.29 , pp. 9004-9009
    • Kumar, H.1    Finer-Moore, J.S.2    Kaback, H.R.3    Stroud, R.M.4
  • 20
    • 80755122853 scopus 로고    scopus 로고
    • Lactose permease and the alternating access mechanism
    • Smirnova I, Kasho V, Kaback HR (2011) Lactose permease and the alternating access mechanism. Biochemistry 50(45): 9684-9693.
    • (2011) Biochemistry , vol.50 , Issue.45 , pp. 9684-9693
    • Smirnova, I.1    Kasho, V.2    Kaback, H.R.3
  • 21
    • 76049089794 scopus 로고    scopus 로고
    • Probing of the rates of alternating access in LacY with Trp fluorescence
    • Smirnova I, Kasho V, Sugihara J, Kaback HR (2009) Probing of the rates of alternating access in LacY with Trp fluorescence. Proc Natl Acad Sci USA 106(51): 21561-21566.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.51 , pp. 21561-21566
    • Smirnova, I.1    Kasho, V.2    Sugihara, J.3    Kaback, H.R.4
  • 22
    • 80053056248 scopus 로고    scopus 로고
    • Opening the periplasmic cavity in lactose permease is the limiting step for sugar binding
    • Smirnova I, Kasho V, Sugihara J, Kaback HR (2011) Opening the periplasmic cavity in lactose permease is the limiting step for sugar binding. Proc Natl Acad Sci USA 108(37): 15147-15151.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.37 , pp. 15147-15151
    • Smirnova, I.1    Kasho, V.2    Sugihara, J.3    Kaback, H.R.4
  • 23
  • 24
    • 0021269079 scopus 로고
    • Purified reconstituted lac carrier protein from Escherichia coli is fully functional
    • Viitanen P, Garcia ML, Kaback HR (1984) Purified reconstituted lac carrier protein from Escherichia coli is fully functional. Proc Natl Acad Sci USA 81(6): 1629-1633.
    • (1984) Proc Natl Acad Sci USA , vol.81 , Issue.6 , pp. 1629-1633
    • Viitanen, P.1    Garcia, M.L.2    Kaback, H.R.3
  • 25
    • 80051658642 scopus 로고    scopus 로고
    • Crystal structure of the ß2 adrenergic receptor-Gs protein complex
    • Rasmussen SG, et al. (2011) Crystal structure of the ß2 adrenergic receptor-Gs protein complex. Nature 477(7366): 549-555.
    • (2011) Nature , vol.477 , Issue.7366 , pp. 549-555
    • Rasmussen, S.G.1
  • 26
    • 80052083563 scopus 로고    scopus 로고
    • Nanobody stabilization of G protein-coupled receptor conformational states
    • Steyaert J, Kobilka BK (2011) Nanobody stabilization of G protein-coupled receptor conformational states. Curr Opin Struct Biol 21(4): 567-572.
    • (2011) Curr Opin Struct Biol , vol.21 , Issue.4 , pp. 567-572
    • Steyaert, J.1    Kobilka, B.K.2
  • 27
    • 84878935042 scopus 로고    scopus 로고
    • Nanobodies: Natural single-domain antibodies
    • Muyldermans S (2013) Nanobodies: Natural single-domain antibodies. Annu Rev Biochem 82: 775-797.
    • (2013) Annu Rev Biochem , vol.82 , pp. 775-797
    • Muyldermans, S.1
  • 28
    • 84886947656 scopus 로고    scopus 로고
    • Adrenaline-activated structure of ß2-adrenoceptor stabilized by an engineered nanobody
    • Ring AM, et al. (2013) Adrenaline-activated structure of ß2-adrenoceptor stabilized by an engineered nanobody. Nature 502(7472): 575-579.
    • (2013) Nature , vol.502 , Issue.7472 , pp. 575-579
    • Ring, A.M.1
  • 29
    • 84894049358 scopus 로고    scopus 로고
    • Regulation of ß2-adrenergic receptor function by conformationally selective single-domain intrabodies
    • Staus DP, et al. (2014) Regulation of ß2-adrenergic receptor function by conformationally selective single-domain intrabodies. Mol Pharmacol 85(3): 472-481.
    • (2014) Mol Pharmacol , vol.85 , Issue.3 , pp. 472-481
    • Staus, D.P.1
  • 30
    • 84924299914 scopus 로고    scopus 로고
    • Outward-facing conformers of LacY stabilized by nanobodies
    • Smirnova I, et al. (2014) Outward-facing conformers of LacY stabilized by nanobodies. Proc Natl Acad Sci USA 111(52): 18548-18553.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.52 , pp. 18548-18553
    • Smirnova, I.1
  • 31
    • 84946962991 scopus 로고    scopus 로고
    • Transient conformers of LacY are trapped by nanobodies
    • Smirnova I, et al. (2015) Transient conformers of LacY are trapped by nanobodies. Proc Natl Acad Sci USA 112(45): 13839-13844.
    • (2015) Proc Natl Acad Sci USA , vol.112 , Issue.45 , pp. 13839-13844
    • Smirnova, I.1
  • 32
    • 33845945208 scopus 로고    scopus 로고
    • Direct sugar binding to LacY measured by resonance energy transfer
    • Smirnova IN, Kasho VN, Kaback HR (2006) Direct sugar binding to LacY measured by resonance energy transfer. Biochemistry 45(51): 15279-15287.
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15279-15287
    • Smirnova, I.N.1    Kasho, V.N.2    Kaback, H.R.3
  • 33
    • 0021774464 scopus 로고
    • Monoclonal antibodies against the lac carrier protein from Escherichia coli. 2. Binding studies with membrane vesicles and proteoliposomes reconstituted with purified lac carrier protein
    • Herzlinger D, Viitanen P, Carrasco N, Kaback HR (1984) Monoclonal antibodies against the lac carrier protein from Escherichia coli. 2. Binding studies with membrane vesicles and proteoliposomes reconstituted with purified lac carrier protein. Biochemistry 23(16): 3688-3693.
    • (1984) Biochemistry , vol.23 , Issue.16 , pp. 3688-3693
    • Herzlinger, D.1    Viitanen, P.2    Carrasco, N.3    Kaback, H.R.4
  • 34
    • 0028200090 scopus 로고
    • Cysteine-scanning mutagenesis of putative helix VII in the lactose permease of Escherichia coli
    • Frillingos S, Sahin-Tóth M, Persson B, Kaback HR (1994) Cysteine-scanning mutagenesis of putative helix VII in the lactose permease of Escherichia coli. Biochemistry 33(26): 8074-8081.
    • (1994) Biochemistry , vol.33 , Issue.26 , pp. 8074-8081
    • Frillingos, S.1    Sahin-Tóth, M.2    Persson, B.3    Kaback, H.R.4
  • 35
    • 0034609555 scopus 로고    scopus 로고
    • Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix VII
    • Venkatesan P, Kwaw I, Hu Y, Kaback HR (2000) Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix VII. Biochemistry 39(35): 10641-10648.
    • (2000) Biochemistry , vol.39 , Issue.35 , pp. 10641-10648
    • Venkatesan, P.1    Kwaw, I.2    Hu, Y.3    Kaback, H.R.4
  • 36
    • 84863369867 scopus 로고    scopus 로고
    • Evidence for an intermediate conformational state of LacY
    • Jiang X, et al. (2012) Evidence for an intermediate conformational state of LacY. Proc Natl Acad Sci USA 109(12): E698-E704.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.12 , pp. E698-E704
    • Jiang, X.1
  • 37
    • 0028206024 scopus 로고
    • Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli
    • Sahin-Tóth M, Persson B, Schwieger J, Cohan P, Kaback HR (1994) Cysteine scanning mutagenesis of the N-terminal 32 amino acid residues in the lactose permease of Escherichia coli. Protein Sci 3(2): 240-247.
    • (1994) Protein Sci , vol.3 , Issue.2 , pp. 240-247
    • Sahin-Tóth, M.1    Persson, B.2    Schwieger, J.3    Cohan, P.4    Kaback, H.R.5
  • 38
    • 0031717187 scopus 로고    scopus 로고
    • Cys-scanning mutagenesis: A novel approach to structure-function relationships in polytopic membrane proteins
    • Frillingos S, Sahin-Tóth M, Wu J, Kaback HR (1998) Cys-scanning mutagenesis: A novel approach to structure-function relationships in polytopic membrane proteins. FASEB J 12(13): 1281-1299.
    • (1998) FASEB J , vol.12 , Issue.13 , pp. 1281-1299
    • Frillingos, S.1    Sahin-Tóth, M.2    Wu, J.3    Kaback, H.R.4
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67(Pt 4): 235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 42
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2): 213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1


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