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Volumn 288, Issue 42, 2013, Pages 30763-30772

Assessing the conformational changes of pb5, the receptor-binding protein of phage T5, upon binding to its escherichia coli receptor FhuA

Author keywords

[No Author keywords available]

Indexed keywords

CELL WALLS; CONFORMATIONAL CHANGE; MEMBRANE RECEPTORS; PHAGE T5; RECEPTOR-BINDING PROTEINS;

EID: 84886912484     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.501536     Document Type: Article
Times cited : (38)

References (54)
  • 1
    • 78650045540 scopus 로고    scopus 로고
    • The phage-host arms race. Shaping the evolution of microbes
    • Stern, A., and Sorek, R. (2011) The phage-host arms race. Shaping the evolution of microbes. BioEssays 33, 43-51
    • (2011) BioEssays , vol.33 , pp. 43-51
    • Stern, A.1    Sorek, R.2
  • 2
    • 77956651527 scopus 로고    scopus 로고
    • Virus hybrids as nanomaterials for biotechnology
    • Soto, C. M., and Ratna, B. R. (2010) Virus hybrids as nanomaterials for biotechnology. Curr. Opin. Biotechnol. 21, 426-438
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 426-438
    • Soto, C.M.1    Ratna, B.R.2
  • 3
    • 79954671431 scopus 로고    scopus 로고
    • Bacteriophages as twenty-first century antibacterial tools for food and medicine
    • Maura, D., and Debarbieux, L. (2011) Bacteriophages as twenty-first century antibacterial tools for food and medicine. Appl. Microbiol. Biotechnol. 90, 851-859
    • (2011) Appl. Microbiol. Biotechnol. , vol.90 , pp. 851-859
    • Maura, D.1    Debarbieux, L.2
  • 4
    • 18744413013 scopus 로고    scopus 로고
    • Bacteriophage therapy. Food and agriculture. Testing grounds for phage therapy
    • Stone, R. (2002) Bacteriophage therapy. Food and agriculture. Testing grounds for phage therapy. Science 298, 730
    • (2002) Science , vol.298 , pp. 730
    • Stone, R.1
  • 6
    • 0021324553 scopus 로고
    • O antigen-dependent mutant of bacteriophage T5
    • Heller, K. J., and Bryniok, D. (1984) O antigen-dependent mutant of bacteriophage T5. J. Virol. 49, 20-25
    • (1984) J. Virol. , vol.49 , pp. 20-25
    • Heller, K.J.1    Bryniok, D.2
  • 7
    • 0010287406 scopus 로고    scopus 로고
    • Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane
    • Boulanger, P., le Maire, M., Bonhivers, M., Dubois, S., Desmadril, M., and Letellier, L. (1996) Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane. Biochemistry 35, 14216-14224
    • (1996) Biochemistry , vol.35 , pp. 14216-14224
    • Boulanger, P.1    Le Maire, M.2    Bonhivers, M.3    Dubois, S.4    Desmadril, M.5    Letellier, L.6
  • 8
    • 0036308517 scopus 로고    scopus 로고
    • Characterization of a high-affinity complex between the bacterial outer membrane protein FhuA and the phage T5 protein pb5
    • Plançon, L., Janmot, C., le Maire, M., Desmadril, M., Bonhivers, M., Letellier, L., and Boulanger, P. (2002) Characterization of a high-affinity complex between the bacterial outer membrane protein FhuA and the phage T5 protein pb5. J. Mol. Biol. 318, 557-569
    • (2002) J. Mol. Biol. , vol.318 , pp. 557-569
    • Plançon, L.1    Janmot, C.2    Le Maire, M.3    Desmadril, M.4    Bonhivers, M.5    Letellier, L.6    Boulanger, P.7
  • 9
    • 66149151407 scopus 로고    scopus 로고
    • FhuA (TonA), the career of a protein
    • Braun, V. (2009) FhuA (TonA), the career of a protein. J. Bacteriol. 191, 3431-3436
    • (2009) J. Bacteriol. , vol.191 , pp. 3431-3436
    • Braun, V.1
  • 10
    • 84864288397 scopus 로고    scopus 로고
    • New insights into pb5, the receptor binding protein of bacteriophage T5, and its interaction with its Escherichia coli receptor FhuA
    • Flayhan, A., Wien, F., Paternostre, M., Boulanger, P., and Breyton, C. (2012) New insights into pb5, the receptor binding protein of bacteriophage T5, and its interaction with its Escherichia coli receptor FhuA. Biochimie 94, 1982-1989
    • (2012) Biochimie 94 , pp. 1982-1989
    • Flayhan, A.1    Wien, F.2    Paternostre, M.3    Boulanger, P.4    Breyton, C.5
  • 12
    • 0001339660 scopus 로고
    • The study of biological structures by neutron scattering from solution
    • Jacrot, B. (1976) The study of biological structures by neutron scattering from solution. Rep. Prog. Phys. 39, 911
    • (1976) Rep. Prog. Phys. , vol.39 , pp. 911
    • Jacrot, B.1
  • 13
    • 0023835926 scopus 로고
    • Low resolution structures of biological complexes studied by neutron scattering
    • Timmins, P. A., and Zaccai, G. (1988) Low resolution structures of biological complexes studied by neutron scattering. Eur. Biophys. J. 15, 257-268
    • (1988) Eur. Biophys. J. , vol.15 , pp. 257-268
    • Timmins, P.A.1    Zaccai, G.2
  • 14
    • 84855784885 scopus 로고    scopus 로고
    • Production of UCP1 a membrane protein from the inner mitochondrial membrane using the cell free expression system in the presence of a fluorinated surfactant
    • Blesneac, I., Ravaud, S., Juillan-Binard, C., Barret, L.-A., Zoonens, M., Polidori, A., Miroux, B., Pucci, B., and Pebay-Peyroula, E. (2012) Production of UCP1 a membrane protein from the inner mitochondrial membrane using the cell free expression system in the presence of a fluorinated surfactant. Biochim. Biophys. Acta 1818, 798-805
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 798-805
    • Blesneac, I.1    Ravaud, S.2    Juillan-Binard, C.3    Barret, L.-A.4    Zoonens, M.5    Polidori, A.6    Miroux, B.7    Pucci, B.8    Pebay-Peyroula, E.9
  • 15
    • 77950465278 scopus 로고    scopus 로고
    • Amphipols and fluorinated surfactants. Two alternatives to detergents for studying membrane proteins in vitro
    • Breyton, C., Pucci, B., and Popot, J.-L. (2010) Amphipols and fluorinated surfactants. Two alternatives to detergents for studying membrane proteins in vitro. Methods Mol. Biol. 601, 219-245
    • (2010) Methods Mol. Biol , vol.601 , pp. 219-245
    • Breyton, C.1    Pucci, B.2    Popot, J.-L.3
  • 16
    • 84874367835 scopus 로고    scopus 로고
    • Hemifluorinated maltoseneopentyl glycol (HF-MNG) amphiphiles for membrane protein stabilisation
    • Cho, K. H., Byrne, B., and Chae, P. S. (2013) Hemifluorinated maltoseneopentyl glycol (HF-MNG) amphiphiles for membrane protein stabilisation. Chembiochem 14, 452-455
    • (2013) Chembiochem , vol.14 , pp. 452-455
    • Cho, K.H.1    Byrne, B.2    Chae, P.S.3
  • 18
    • 70349909646 scopus 로고    scopus 로고
    • Hydrogenated and fluorinated surfactants derived from tris(hydroxymethyl)-acrylamidomethane allow the purification of a highly active yeast F1-F0 ATP-synthase with an enhanced stability
    • Talbot, J.-C., Dautant, A., Polidori, A., Pucci, B., Cohen-Bouhacina, T., Maali, A., Salin, B., Brèthes, D., Velours, J., and Giraud, M.-F. (2009) Hydrogenated and fluorinated surfactants derived from tris(hydroxymethyl)- acrylamidomethane allow the purification of a highly active yeast F1-F0 ATP-synthase with an enhanced stability. J. Bioenerg. Biomembr. 41, 349-360
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 349-360
    • Talbot, J.-C.1    Dautant, A.2    Polidori, A.3    Pucci, B.4    Cohen-Bouhacina, T.5    Maali, A.6    Salin, B.7    Brèthes, D.8    Velours, J.9    Giraud, M.-F.10
  • 19
    • 55249110802 scopus 로고    scopus 로고
    • Glucose-based surfactants with hydrogenated, fluorinated, or hemifluorinated tails. Synthesis and comparative physical-chemical characterization
    • Abla, M., Durand, G., and Pucci, B. (2008) Glucose-based surfactants with hydrogenated, fluorinated, or hemifluorinated tails. Synthesis and comparative physical-chemical characterization. J. Org. Chem. 73, 8142-8153
    • (2008) J. Org. Chem. , vol.73 , pp. 8142-8153
    • Abla, M.1    Durand, G.2    Pucci, B.3
  • 20
    • 69349089410 scopus 로고    scopus 로고
    • Micellar and biochemical properties of (hemi)fluorinated surfactants are controlled by the size of the polar head
    • Breyton, C., Gabel, F., Abla, M., Pierre, Y., Lebaupain, F., Durand, G., Popot, J.-L., Ebel, C., and Pucci, B. (2009) Micellar and biochemical properties of (hemi)fluorinated surfactants are controlled by the size of the polar head. Biophys. J. 97, 1077-1086
    • (2009) Biophys. J. , vol.97 , pp. 1077-1086
    • Breyton, C.1    Gabel, F.2    Abla, M.3    Pierre, Y.4    Lebaupain, F.5    Durand, G.6    Popot, J.-L.7    Ebel, C.8    Pucci, B.9
  • 21
    • 84856083585 scopus 로고    scopus 로고
    • A diglucosylated fluorinated surfactant to handle integral membrane proteins in aqueous solution
    • Abla, M., Durand, G., Breyton, C., Raynal, S., Ebel, C., and Pucci, B. (2012) A diglucosylated fluorinated surfactant to handle integral membrane proteins in aqueous solution. J. Fluor. Chem. 134, 63-71
    • (2012) J. Fluor. Chem. , vol.134 , pp. 63-71
    • Abla, M.1    Durand, G.2    Breyton, C.3    Raynal, S.4    Ebel, C.5    Pucci, B.6
  • 22
    • 0031822853 scopus 로고    scopus 로고
    • An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein fro
    • Ferguson, A. D., Breed, J., Diederichs, K., Welte, W., and Coulton, J. W. (1998) An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12. Protein Sci. 7, 1636-1638
    • (1998) Escherichia Coli K-12. Protein Sci. , vol.7 , pp. 1636-1638
    • Ferguson, A.D.1    Breed, J.2    Diederichs, K.3    Welte, W.4    Coulton, J.W.5
  • 23
    • 79955615219 scopus 로고    scopus 로고
    • Sedimentation velocity to characterize surfactants and solubilized membrane proteins
    • Ebel, C. (2011) Sedimentation velocity to characterize surfactants and solubilized membrane proteins. Methods 54, 56-66
    • (2011) Methods , vol.54 , pp. 56-66
    • Ebel, C.1
  • 24
    • 77954615206 scopus 로고    scopus 로고
    • Analytical ultracentrifugation sedimentation velocity for the characterization of detergent-solubilized membrane proteins Ca2-ATPase and ExbB
    • Salvay, A. G., Santamaria, M., le Maire, M., and Ebel, C. (2007) Analytical ultracentrifugation sedimentation velocity for the characterization of detergent-solubilized membrane proteins Ca2-ATPase and ExbB. J. Biol. Phys. 33, 399-419
    • (2007) J. Biol. Phys. , vol.33 , pp. 399-419
    • Salvay, A.G.1    Santamaria, M.2    Le Maire, M.3    Ebel, C.4
  • 27
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • Jacrot, B., and Zaccai, G. (1981) Determination of molecular weight by neutron scattering. Biopolymers 20, 2413-2426
    • (1981) Biopolymers , vol.20 , pp. 2413-2426
    • Jacrot, B.1    Zaccai, G.2
  • 28
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid abinitio shape determination in small-angle scattering
    • Franke, D., and Svergun, D. I. (2009) DAMMIF, a program for rapid abinitio shape determination in small-angle scattering. J. Appl. Crystallogr. 42, 342-346
    • (2009) J. Appl. Crystallogr , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 29
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 30
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V., and Svergun, D. I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-864
    • (2003) J. Appl. Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 32
    • 0033377664 scopus 로고    scopus 로고
    • EMAN. Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R., and Chiu, W. (1999) EMAN. Semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 33
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle x-ray solution scattering
    • Mertens, H. D., and Svergun, D. I. (2010) Structural characterization of proteins and complexes using small-angle x-ray solution scattering. J. Struct. Biol. 172, 128-141
    • (2010) J. Struct. Biol. , vol.172 , pp. 128-141
    • Mertens, H.D.1    Svergun, D.I.2
  • 34
    • 79960670728 scopus 로고    scopus 로고
    • Low resolution structure of a bacterial SLC26 transporter reveals dimeric stoichiometry and mobile intracellular domains
    • Compton, E. L., Karinou, E., Naismith, J. H., Gabel, F., and Javelle, A. (2011) Low resolution structure of a bacterial SLC26 transporter reveals dimeric stoichiometry and mobile intracellular domains. J. Biol. Chem. 286, 27058-27067
    • (2011) J. Biol. Chem. , vol.286 , pp. 27058-27067
    • Compton, E.L.1    Karinou, E.2    Naismith, J.H.3    Gabel, F.4    Javelle, A.5
  • 36
    • 84877778935 scopus 로고    scopus 로고
    • Super-resolution in solution X-ray scattering and its applications to structural systems biology
    • Rambo, R. P., and Tainer, J. A. (2013) Super-resolution in solution X-ray scattering and its applications to structural systems biology. Annu. Rev. Biophys. 42, 415-441
    • (2013) Annu. Rev. Biophys. , vol.42 , pp. 415-441
    • Rambo, R.P.1    Tainer, J.A.2
  • 37
    • 84867502987 scopus 로고    scopus 로고
    • TonB-dependent transporter FhuA in planar lipid bilayers. Partial exit of its plug from the barrel
    • Udho, E., Jakes, K. S., and Finkelstein, A. (2012) TonB-dependent transporter FhuA in planar lipid bilayers. Partial exit of its plug from the barrel. Biochemistry 51, 6753-6759
    • (2012) Biochemistry , vol.51 , pp. 6753-6759
    • Udho, E.1    Jakes, K.S.2    Finkelstein, A.3
  • 38
    • 0035822681 scopus 로고    scopus 로고
    • FhuA-mediated phage genome transfer into liposomes. A cryo-electron tomography study
    • Böhm, J., Lambert, O., Frangakis, A. S., Letellier, L., Baumeister, W., and Rigaud, J. L. (2001) FhuA-mediated phage genome transfer into liposomes. A cryo-electron tomography study. Curr. Biol. 11, 1168-1175
    • (2001) Curr. Biol. , vol.11 , pp. 1168-1175
    • Böhm, J.1    Lambert, O.2    Frangakis, A.S.3    Letellier, L.4    Baumeister, W.5    Rigaud, J.L.6
  • 39
    • 84884556983 scopus 로고    scopus 로고
    • TssK is a trimeric cytoplasmic protein interacting with components of both phage-like and membrane anchoring complexes of the Type VI secretion system
    • Zoued,A., Durand, E., Bebeacua, C., Brunet, Y. R., Douzi, B., Cambillau, C., Cascales, E., and Journet, L. (2013) TssK is a trimeric cytoplasmic protein interacting with components of both phage-like and membrane anchoring complexes of the Type VI secretion system. J. Biol. Chem. 288, 27031-27041
    • (2013) J. Biol. Chem. , vol.288 , pp. 27031-27041
    • Zoued, A.1    Durand, E.2    Bebeacua, C.3    Brunet, Y.R.4    Douzi, B.5    Cambillau, C.6    Cascales, E.7    Journet, L.8
  • 40
    • 80052206993 scopus 로고    scopus 로고
    • A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries
    • Veesler, D., and Cambillau, C. (2011) A common evolutionary origin for tailed-bacteriophage functional modules and bacterial machineries. Microbiol. Mol. Biol. Rev. 75, 423-433
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 423-433
    • Veesler, D.1    Cambillau, C.2
  • 45
    • 84855759113 scopus 로고    scopus 로고
    • Role of bacteriophage SPP1 tail spike protein gp21 on host cell receptor binding and trigger of phageDNAejection
    • Vinga, I., Baptista, C., Auzat, I., Petipas, I., Lurz, R., Tavares, P., Santos, M. A., and São-José, C. (2012) Role of bacteriophage SPP1 tail spike protein gp21 on host cell receptor binding and trigger of phageDNAejection. Mol. Microbiol. 83, 289-303
    • (2012) Mol. Microbiol. , vol.83 , pp. 289-303
    • Vinga, I.1    Baptista, C.2    Auzat, I.3    Petipas, I.4    Lurz, R.5    Tavares, P.6    Santos, M.A.7    São-José, C.8
  • 46
    • 77956892290 scopus 로고    scopus 로고
    • Visualizing the structural changes of bacteriophage 15 and its Salmonella host during infection
    • Chang, J. T., Schmid, M. F., Haase-Pettingell, C., Weigele, P. R., King, J. A., and Chiu, W. (2010) Visualizing the structural changes of bacteriophage 15 and its Salmonella host during infection. J. Mol. Biol. 402, 731-740
    • (2010) J. Mol. Biol , vol.402 , pp. 731-740
    • Chang, J.T.1    Schmid, M.F.2    Haase-Pettingell, C.3    Weigele, P.R.4    King, J.A.5    Chiu, W.6
  • 49
  • 50
    • 0033985920 scopus 로고    scopus 로고
    • The C-terminal portion of the tail fiber protein of bacteriophage is responsible for binding to LamB, its receptor at the surface of Escherichia coli K-12
    • Wang, J., Hofnung, M., and Charbit, A. (2000) The C-terminal portion of the tail fiber protein of bacteriophage is responsible for binding to LamB, its receptor at the surface of Escherichia coli K-12. J. Bacteriol. 182, 508-512
    • (2000) J. Bacteriol , vol.182 , pp. 508-512
    • Wang, J.1    Hofnung, M.2    Charbit, A.3
  • 51
    • 33744962964 scopus 로고    scopus 로고
    • The ectodomain of the viral receptor YueB forms a fiber that triggers ejection of bacteriophage SPP1 DNA
    • São-José, C., Lhuillier, S., Lurz, R., Melki, R., Lepault, J., Santos, M. A., and Tavares, P. (2006) The ectodomain of the viral receptor YueB forms a fiber that triggers ejection of bacteriophage SPP1 DNA. J. Biol. Chem. 281, 11464-11470
    • (2006) J. Biol. Chem. , vol.281 , pp. 11464-11470
    • São-José, C.1    Lhuillier, S.2    Lurz, R.3    Melki, R.4    Lepault, J.5    Santos, M.A.6    Tavares, P.7
  • 52
    • 0024720285 scopus 로고
    • A component of the side tail fiber of Escherichia coli bacteriophage can functionally replace the receptor-recognizing part of a long tail fiber protein of the unrelated bacteriophage T4
    • Montag, D., Schwarz, H., and Henning, U. (1989) A component of the side tail fiber of Escherichia coli bacteriophage can functionally replace the receptor-recognizing part of a long tail fiber protein of the unrelated bacteriophage T4. J. Bacteriol. 171, 4378-4384
    • (1989) J. Bacteriol , vol.171 , pp. 4378-4384
    • Montag, D.1    Schwarz, H.2    Henning, U.3
  • 53
    • 0020699587 scopus 로고
    • Injection of DNA into liposomes by bacteriophage
    • Roessner, C. A., Struck, D. K., and Ihler, G. M. (1983) Injection of DNA into liposomes by bacteriophage. J. Biol. Chem. 258, 643-648
    • (1983) J. Biol. Chem. , vol.258 , pp. 643-648
    • Roessner, C.A.1    Struck, D.K.2    Ihler, G.M.3


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