메뉴 건너뛰기




Volumn 12, Issue 3, 2003, Pages 577-585

Crystal structure of a defective folding protein

Author keywords

Crystal structure; Maltose transport; Maltose binding protein; Periplasm; Protein misfolding

Indexed keywords

ASPARTIC ACID; CHAPERONE; GLYCINE; ISOLEUCINE; MALTOSE BINDING PROTEIN; PROLINE;

EID: 0037369139     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0235103     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arie, J.-P., Sassoon, N., and Betton, J.-M. 2001. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 39: 199-210.
    • (2001) Mol. Microbiol. , vol.39 , pp. 199-210
    • Arie, J.-P.1    Sassoon, N.2    Betton, J.-M.3
  • 2
    • 0029923189 scopus 로고    scopus 로고
    • Folding of a mutant maltose binding protein of E. coli which forms inclusion bodies
    • Betton, J.-M. and Hofnung, M. 1996. Folding of a mutant maltose binding protein of E. coli which forms inclusion bodies. J Biol. Chem. 271: 8046-8052.
    • (1996) J Biol. Chem. , vol.271 , pp. 8046-8052
    • Betton, J.-M.1    Hofnung, M.2
  • 3
    • 0030595346 scopus 로고    scopus 로고
    • Probing the structural role of an ab loop of maltose-binding protein by mutagenesis: Heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies
    • Betton, J.-M., Boscus, D., Missiakas, D., Raina, S., and Hofnung, M. 1996. Probing the structural role of an ab loop of maltose-binding protein by mutagenesis: Heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies. J. Mol. Biol. 262: 140-150.
    • (1996) J. Mol. Biol. , vol.262 , pp. 140-150
    • Betton, J.-M.1    Boscus, D.2    Missiakas, D.3    Raina, S.4    Hofnung, M.5
  • 4
    • 0032502781 scopus 로고    scopus 로고
    • Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli
    • Betton, J.-M., Sassoon, N., Hofnung, M., and Laurent, M. 1998. Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli. J. Biol. Chem. 273: 8897-8902.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8897-8902
    • Betton, J.-M.1    Sassoon, N.2    Hofnung, M.3    Laurent, M.4
  • 5
    • 0033153294 scopus 로고    scopus 로고
    • There's a right way and a wrong way: In vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike
    • Betts, S. and King, J. 1999. There's a right way and a wrong way: In vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike. Structure 7: R131-R139.
    • (1999) Structure , vol.7
    • Betts, S.1    King, J.2
  • 6
    • 0031887807 scopus 로고    scopus 로고
    • Maltose/maltodextrin system of Escherichia coli: Transport, metabolism, and regulation
    • Boos, W. and Shuman, H. 1998. Maltose/maltodextrin system of Escherichia coli: Transport, metabolism, and regulation. Microbiol. Mol. Biol. Rev. 62: 204-229.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 204-229
    • Boos, W.1    Shuman, H.2
  • 7
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen, J., Sharma, S., Quiocho, F.A., and Davidson, A.L. 2001. Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport. Proc. Natl. Acad. Sci. 98: 1525-1530.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 8
    • 0032432109 scopus 로고    scopus 로고
    • Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli
    • Danese, P.N. and Silhavy, T.J. 1998. Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli. Annu. Rev. Genet. 32: 59-94.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 59-94
    • Danese, P.N.1    Silhavy, T.J.2
  • 9
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins
    • Davidson, A.L., Shuman, H.A., and Nikaido, H. 1992. Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins. Proc. Natl. Acad. Sci. 89: 2360-2364.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 10
    • 0018076641 scopus 로고
    • Dominant constitutive mutations in malT, the positive regulator gene of the maltose regulon in Escherichia coli
    • Debarbouille, M., Shuman, H.A., Silhavy, T.J., and Schwartz, M. 1978. Dominant constitutive mutations in malT, the positive regulator gene of the maltose regulon in Escherichia coli. J. Mol. Biol. 124: 359-371.
    • (1978) J. Mol. Biol. , vol.124 , pp. 359-371
    • Debarbouille, M.1    Shuman, H.A.2    Silhavy, T.J.3    Schwartz, M.4
  • 11
    • 0035830955 scopus 로고    scopus 로고
    • Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: Flexibility of tertiary structure and ligand binding
    • Duan, X., Hall, J.A., Nikaido, H., and Quiocho, F.A. 2001. Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: Flexibility of tertiary structure and ligand binding. J. Mol. Biol. 306: 1115-1126.
    • (2001) J. Mol. Biol. , vol.306 , pp. 1115-1126
    • Duan, X.1    Hall, J.A.2    Nikaido, H.3    Quiocho, F.A.4
  • 12
    • 0023274512 scopus 로고
    • Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12
    • Duplay, P., Szmelcman, S., Bedouelle, H., and Hofnung, M. 1987. Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. J. Mol. Biol. 194: 663-673.
    • (1987) J. Mol. Biol. , vol.194 , pp. 663-673
    • Duplay, P.1    Szmelcman, S.2    Bedouelle, H.3    Hofnung, M.4
  • 13
    • 0023883586 scopus 로고
    • Formation of aggregates from thermolabile in-vivo folding intermediate in P22 tailspike maturation
    • Haase-Pettingell, C.A. and King, J. 1988. Formation of aggregates from thermolabile in-vivo folding intermediate in P22 tailspike maturation. J. Biol. Chem. 263: 4977-4983.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4977-4983
    • Haase-Pettingell, C.A.1    King, J.2
  • 14
    • 0027490784 scopus 로고
    • Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex
    • Hor, L.I. and Shuman, H.A. 1993. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex. J. Mol. Biol. 233: 659-670.
    • (1993) J. Mol. Biol. , vol.233 , pp. 659-670
    • Hor, L.I.1    Shuman, H.A.2
  • 15
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the locadon of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. 1991. Improved methods for binding protein models in electron density maps and the locadon of errors in these models. Acta Crystallogr. A 47: 110-120.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-120
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0024519269 scopus 로고
    • Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures
    • Lipinska, B., Fayet, O., Baird, L., and Georgopoulos, C. 1989. Identification, characterization, and mapping of the Escherichia coli htrA gene. whose product is essential for bacterial growth only at elevated temperatures. J. Bacteriol. 171: 1574-1584.
    • (1989) J. Bacteriol. , vol.171 , pp. 1574-1584
    • Lipinska, B.1    Fayet, O.2    Baird, L.3    Georgopoulos, C.4
  • 17
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur, M.W. and Thornton, J.M. 1991. Influence of proline residues on protein conformation. J. Mol. Biol. 218: 397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 18
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas, D., Betton, J.-M., and Raina, S. 1996. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol. Microbiol. 21: 871-884.
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.-M.2    Raina, S.3
  • 19
    • 0025850262 scopus 로고
    • Global suppression of protein folding defects and inclusion body formation
    • Mitraki, A., Fane, B., Haase-Pettingell, C., Sturtevant, J., and King, J. 1991. Global suppression of protein folding defects and inclusion body formation. Science 253: 54-58.
    • (1991) Science , vol.253 , pp. 54-58
    • Mitraki, A.1    Fane, B.2    Haase-Pettingell, C.3    Sturtevant, J.4    King, J.5
  • 20
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M., Hofnung, M., and Dassa, E. 1997. Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 16: 3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 21
    • 0031756353 scopus 로고    scopus 로고
    • In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: Modulation by ATP
    • Mourez, M., Jehanno, M., Schneider, E., and Dassa, E. 1998. In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: Modulation by ATP. Mol. Microbiol. 30: 353-363.
    • (1998) Mol. Microbiol. , vol.30 , pp. 353-363
    • Mourez, M.1    Jehanno, M.2    Schneider, E.3    Dassa, E.4
  • 22
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of molecular structures by the maximum likelihood method
    • Murshudov, G.N., Vagin, A.A., and Dodson, E.J. 1997. Refinement of molecular structures by the maximum likelihood method. Acta Crystallogr. D 53: 240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 23
    • 84920325457 scopus 로고
    • AMORE: An automated package for molecular replacement
    • Navaza, J. 1994. AMORE: An automated package for molecular replacement. Acta Crystallogr. A 50: 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 24
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu, H.C. and Heppel, L.A. 1965. The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J. Biol. Chem. 240: 3685-3692.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, M. 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, M.2
  • 26
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho, F.A., Spurlino, J.C., and Rodseth, L.E. 1997. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure 5: 997-1015.
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 27
    • 0031764460 scopus 로고    scopus 로고
    • Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein
    • Raffy, S., Sassoon, N., Hofnung, H., and Betton, J.-M. 1998. Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein. Protein Sci. 7: 2136-2142.
    • (1998) Protein Sci. , vol.7 , pp. 2136-2142
    • Raffy, S.1    Sassoon, N.2    Hofnung, H.3    Betton, J.-M.4
  • 28
    • 13144256689 scopus 로고    scopus 로고
    • Crystal structure of a dominant B-cell epitope from the preS2 region of hepatitis B virus in the form of an inserted peptide segment in maltodextrin-binding protein
    • Saul, F.A., Vulliez-le Normand, B., Lema, F., and Bentley, G.A. 1998. Crystal structure of a dominant B-cell epitope from the preS2 region of hepatitis B virus in the form of an inserted peptide segment in maltodextrin-binding protein. J. Mol. Biol. 280: 185-192.
    • (1998) J. Mol. Biol. , vol.280 , pp. 185-192
    • Saul, F.A.1    Vulliez-le Normand, B.2    Lema, F.3    Bentley, G.A.4
  • 29
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • Sharff, A.J., Rodseth, L.E., Spurlino, J.C., and Quiocho, F.A. 1992. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 31: 10657-10663.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 30
    • 0020320406 scopus 로고
    • Active transport of maltose in Escherichia coli K12
    • Shuman, H.A. 1982. Active transport of maltose in Escherichia coli K12. J. Biol. Chem. 257: 5455-5461.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5455-5461
    • Shuman, H.A.1
  • 31
    • 0025754301 scopus 로고
    • The 2.3-Å resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J.C., Lu, G.Y., and Quiocho, F.A. 1991. The 2.3-Å resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266: 5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.Y.2    Quiocho, F.A.3
  • 32
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • Strauch, K.L., Johnson, K., and Beckwith, J. 1989. Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J. Bacteriol. 171: 2689-2696.
    • (1989) J. Bacteriol. , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 33
    • 0029933361 scopus 로고    scopus 로고
    • Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli
    • Sugiyama, S., Vassylyev, D.G., Matsushima, M., Kashiwagi, K., Igarashi, K., and Morikawa, K. 1996. Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli. J. Biol. Chem. 271: 9519-9525.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9519-9525
    • Sugiyama, S.1    Vassylyev, D.G.2    Matsushima, M.3    Kashiwagi, K.4    Igarashi, K.5    Morikawa, K.6
  • 34
    • 0022259474 scopus 로고
    • Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system
    • Treptow, N.A. and Shuman, H.A. 1985. Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system. J. Bacteriol. 163: 654-660.
    • (1985) J. Bacteriol. , vol.163 , pp. 654-660
    • Treptow, N.A.1    Shuman, H.A.2
  • 35
    • 0023787957 scopus 로고
    • Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system
    • -. 1988. Allele-specific malE mutations that restore interactions between maltose-binding protein and the inner-membrane components of the maltose transport system. J. Mol. Biol. 202: 809-822.
    • (1988) J. Mol. Biol. , vol.202 , pp. 809-822


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.