메뉴 건너뛰기




Volumn 5, Issue 8, 1997, Pages 997-1015

Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor

Author keywords

Active transport; Chemotaxis; Maltodextrin binding protein structure; Oligosaccharide conformation; Protein oligosaccharide interactions

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0031571605     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00253-0     Document Type: Article
Times cited : (298)

References (51)
  • 1
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding protein-dependent ABC transporters
    • (Neidhardt, F.C., ed.), ASM Press, Washington, DC
    • Boos, W. & Lucht, J.M. (1996). Periplasmic binding protein-dependent ABC transporters. In Escherichia coli and Salmonella Cellular and Molecular Biology. (Neidhardt, F.C., ed.), pp. 1175-1209, ASM Press, Washington, DC.
    • (1996) Escherichia Coli and Salmonella Cellular and Molecular Biology , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 3
    • 0016151381 scopus 로고
    • Active transport of maltose in Escherichia coli K-1 2. Involvement of a periplasmic maltose-binding protein
    • Kellerman, O. & Szmelcman, S. (1974). Active transport of maltose in Escherichia coli K-1 2. Involvement of a periplasmic maltose-binding protein. Eur. J. Biochem. 47, 139-149.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 139-149
    • Kellerman, O.1    Szmelcman, S.2
  • 4
    • 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. & 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
  • 5
    • 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. & 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
  • 6
    • 0027364214 scopus 로고
    • Refined 1.8 Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein
    • Sharff, A.J., Rodseth, L.E. & Quiocho, F.A. (1993). Refined 1.8 Å structure reveals the mode of binding of β-cyclodextrin to the maltodextrin binding protein. Biochemistry 32, 10553-10559.
    • (1993) Biochemistry , vol.32 , pp. 10553-10559
    • Sharff, A.J.1    Rodseth, L.E.2    Quiocho, F.A.3
  • 7
    • 0021205810 scopus 로고
    • Novel stereospecificity of the L-arabinose-binding protein
    • Quiocho, F.A. & Vyas, N.K. (1984). Novel stereospecificity of the L-arabinose-binding protein. Nature 310, 381-386.
    • (1984) Nature , vol.310 , pp. 381-386
    • Quiocho, F.A.1    Vyas, N.K.2
  • 8
    • 0024375861 scopus 로고
    • Substrate specificity and affinity of a protein modulated by bound water molecules
    • Quiocho, F.A., Wilson, D.K. & Vyas, N.K. (1989). Substrate specificity and affinity of a protein modulated by bound water molecules. Nature 340, 404-407.
    • (1989) Nature , vol.340 , pp. 404-407
    • Quiocho, F.A.1    Wilson, D.K.2    Vyas, N.K.3
  • 9
    • 0024237631 scopus 로고
    • Sugar- And signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein
    • Vyas, N.K., Vyas, M.N. & Quiocho, F.A. (1988). Sugar- and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein. Science 242, 1290-1295.
    • (1988) Science , vol.242 , pp. 1290-1295
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 10
    • 0028244277 scopus 로고
    • Crystallographic analysis of the epimeric, and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose, and D-galactose
    • Vyas, M.N., Vyas, N.K. & Quiocho, F.A. (1994). Crystallographic analysis of the epimeric, and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose, and D-galactose. Biochemistry 33, 4762-4768.
    • (1994) Biochemistry , vol.33 , pp. 4762-4768
    • Vyas, M.N.1    Vyas, N.K.2    Quiocho, F.A.3
  • 11
    • 0027340581 scopus 로고
    • The 1.7 Å refined X-ray structure of the periplasmic glucose/galactose receptor from Salmonella typhimurium
    • Zou, J., Flocco, M.M. & Mowbray, S.L. (1993). The 1.7 Å refined X-ray structure of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J. Mol. Biol. 233, 7399-752.
    • (1993) J. Mol. Biol. , vol.233 , pp. 7399-7752
    • Zou, J.1    Flocco, M.M.2    Mowbray, S.L.3
  • 12
    • 0027112289 scopus 로고
    • 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli
    • 2. Mowbray, S.L. & Cole, L.B. (1992). 1.7 Å X-ray structure of the periplasmic ribose receptor from Escherichia coli. J. Mol. Biol. 225, 155-175.
    • (1992) J. Mol. Biol. , vol.225 , pp. 155-175
    • Mowbray, S.L.1    Cole, L.B.2
  • 13
    • 0018948077 scopus 로고
    • The mechanism of sugar binding to the periplasmic receptor for galactose chemotaxis and transport in Escherichia coli
    • Miller, D.M., Olson, J.S. & Quiocho, F.A. (1980). The mechanism of sugar binding to the periplasmic receptor for galactose chemotaxis and transport in Escherichia coli. J. Biol. Chem. 255, 2465-2471.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2465-2471
    • Miller, D.M.1    Olson, J.S.2    Quiocho, F.A.3
  • 14
    • 0021062151 scopus 로고
    • Rates of ligand binding to periplasmic binding proteins involved in bacterial transport and chemotaxis
    • Miller, D.M., Olson, J.S., Pflugrath, J.W. & Quiocho, F.A. (1983). Rates of ligand binding to periplasmic binding proteins involved in bacterial transport and chemotaxis. J. Biol. Chem. 258, 13193-13198.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13193-13198
    • Miller, D.M.1    Olson, J.S.2    Pflugrath, J.W.3    Quiocho, F.A.4
  • 15
    • 0019254027 scopus 로고
    • The role of the Escherichia coli λ receptor in the transport of maltose and maltodextrins
    • Ferenci, T. & Boos, W. (1980). The role of the Escherichia coli λ receptor in the transport of maltose and maltodextrins. J. Supramol. Struct. 94, 101-116.
    • (1980) J. Supramol. Struct. , vol.94 , pp. 101-116
    • Ferenci, T.1    Boos, W.2
  • 16
    • 0026763292 scopus 로고
    • Atomic interactions in protein-carbohydrate complexes: Tryptophan residues in the periplasmic maltodextrin receptor for transport and chemotaxis
    • Spurlino, J.C., Rodseth, L.E. & Quiocho, F.A. (1992). Atomic interactions in protein-carbohydrate complexes: tryptophan residues in the periplasmic maltodextrin receptor for transport and chemotaxis. J. Mol. Biol. 226, 15-22.
    • (1992) J. Mol. Biol. , vol.226 , pp. 15-22
    • Spurlino, J.C.1    Rodseth, L.E.2    Quiocho, F.A.3
  • 17
    • 0000319698 scopus 로고
    • Atomic structures and function of periplasmic receptors for active transport and chemotaxis
    • Quiocho, F.A. (1991). Atomic structures and function of periplasmic receptors for active transport and chemotaxis. Curr. Opin. Struct. Biol. 1, 922-933.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 922-933
    • Quiocho, F.A.1
  • 18
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F.A. & Ledvina, P.S. (1996). Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol. Microbiol. 20, 17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 19
    • 0029658872 scopus 로고    scopus 로고
    • The 1.8-Å X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding
    • Sugiyama, S., et al., & Morikawa, K. (1996). The 1.8-Å X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding. Protein Sci. 5, 1984-1990.
    • (1996) Protein Sci. , vol.5 , pp. 1984-1990
    • Sugiyama, S.1    Morikawa, K.2
  • 20
    • 0028174670 scopus 로고
    • Refined 1.89 Å structure of the histidine-binding protein complexed with histidine, and its relationship with other active transport/chemosensory proteins
    • Yao, N., Trakhanov, S. & Quiocho, F.A. (1994). Refined 1.89 Å structure of the histidine-binding protein complexed with histidine, and its relationship with other active transport/chemosensory proteins. Biochemistry 33, 4769-4779.
    • (1994) Biochemistry , vol.33 , pp. 4769-4779
    • Yao, N.1    Trakhanov, S.2    Quiocho, F.A.3
  • 22
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas, N.K. (1991). Atomic features of protein-carbohydrate interactions. Curr. Opin. Struct. Biol. 1, 732-740.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 732-740
    • Vyas, N.K.1
  • 23
    • 0027968302 scopus 로고
    • The three-dimensional structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei
    • Divne, C., et al., & Jones, A. (1994). The three-dimensional structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei. Science 265, 524-528.
    • (1994) Science , vol.265 , pp. 524-528
    • Divne, C.1    Jones, A.2
  • 24
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structure of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler, R., Wang, Y.-F., Rizkallah, P.J., Rosenbusch, J.P. & Schirmer, T. (1996). Crystal structure of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4, 127-134.
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.-F.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 25
    • 0001548751 scopus 로고
    • On the importance of orientation in general base catalysis by carboxylate
    • Gandour, R.D. (1981). On the importance of orientation in general base catalysis by carboxylate. Bioorg. Chem. 10, 169-176.
    • (1981) Bioorg. Chem. , vol.10 , pp. 169-176
    • Gandour, R.D.1
  • 26
    • 0022555847 scopus 로고
    • Carbohydrate-binding proteins: Tertiary structures and protein-sugar interactions
    • Quiocho, F.A. (1986). Carbohydrate-binding proteins: tertiary structures and protein-sugar interactions. Annu. Rev. Biochem. 55, 287-315.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 287-315
    • Quiocho, F.A.1
  • 27
    • 49049134955 scopus 로고
    • Crystal and molecular structure of cyclohepta-amylose dodecahydrate
    • Lindner, K. & Saenger, W. (1982). Crystal and molecular structure of cyclohepta-amylose dodecahydrate. Carbohydr. Res. 99, 103-115.
    • (1982) Carbohydr. Res. , vol.99 , pp. 103-115
    • Lindner, K.1    Saenger, W.2
  • 28
    • 0013852463 scopus 로고
    • Structure of hen egg white lysozyme. A three-dimensional Fourier synthesis at 2.0 Å resolution
    • Blake, C.C.F., Koening, D.F., Mair, G.A., North A.C.T., Phillips, D.C. & Sarma, V.R. (1965). Structure of hen egg white lysozyme. A three-dimensional Fourier synthesis at 2.0 Å resolution. Nature 206, 757-761.
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koening, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 29
    • 0013852450 scopus 로고
    • Structure of some crystalline lysozyme-inhibitor complexes determined by X-ray analysis at 5 Å resolution
    • Johnson, L.N. & Phillips, D.C. (1965). Structure of some crystalline lysozyme-inhibitor complexes determined by X-ray analysis at 5 Å resolution. Nature 206, 761-763.
    • (1965) Nature , vol.206 , pp. 761-763
    • Johnson, L.N.1    Phillips, D.C.2
  • 32
    • 0024189319 scopus 로고
    • Molecular features and basic understanding of protein-carbohydrate interactions: The arabinose-binding protein-sugar complex
    • Quiocho, F.A. (1988). Molecular features and basic understanding of protein-carbohydrate interactions: the arabinose-binding protein-sugar complex. Curr. Top. Microbiol. Immunol. 139, 135-148.
    • (1988) Curr. Top. Microbiol. Immunol. , vol.139 , pp. 135-148
    • Quiocho, F.A.1
  • 33
    • 0022525924 scopus 로고
    • Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins
    • Ferenci, T., Muir, M., Lee, K.-S. & Maris, D. (1986). Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins. Biochim. Biophys. Acta 860, 44-50.
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 44-50
    • Ferenci, T.1    Muir, M.2    Lee, K.-S.3    Maris, D.4
  • 34
    • 0022794836 scopus 로고
    • 3-Azi-1-methoxybutyl D-maltooligosaccharides specifically bind to the maltose/maltooligosaccharide-binding protein of Escherichia coli and can be used as photoaffinity labels
    • Thieme, R., Lay, H., Oser, A., Lehmann, J., Wrissenberg, S. & Boos, W. (1986). 3-Azi-1-methoxybutyl D-maltooligosaccharides specifically bind to the maltose/maltooligosaccharide-binding protein of Escherichia coli and can be used as photoaffinity labels. Eur. J. Biochem. 160, 83-91.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 83-91
    • Thieme, R.1    Lay, H.2    Oser, A.3    Lehmann, J.4    Wrissenberg, S.5    Boos, W.6
  • 35
    • 0025813345 scopus 로고
    • Tritium NMR spectroscopy of ligand binding to maltose-binding protein
    • Gehring, K., Williams, P.G., Pelton, J.G., Morimoto, H. & Wemmer, D.E. (1991). Tritium NMR spectroscopy of ligand binding to maltose-binding protein. Biochemistry 30, 5524-5531.
    • (1991) Biochemistry , vol.30 , pp. 5524-5531
    • Gehring, K.1    Williams, P.G.2    Pelton, J.G.3    Morimoto, H.4    Wemmer, D.E.5
  • 36
    • 0003016299 scopus 로고
    • Crystallographic studies of carbohydrates
    • Jeffrey, G.A. (1990). Crystallographic studies of carbohydrates. Acta Cryst. B 46, 89-103.
    • (1990) Acta Cryst. B , vol.46 , pp. 89-103
    • Jeffrey, G.A.1
  • 37
    • 0002188624 scopus 로고
    • Rearrangements and isomerizations in carbohydrate chemistry
    • deMayo, ed., Wiley-lnterscience, New York, NY
    • Lemieux, R.U. (1963). Rearrangements and isomerizations in carbohydrate chemistry. In Molecular Rearrangements. (deMayo, ed.), pp. 713-769, Wiley-lnterscience, New York, NY.
    • (1963) Molecular Rearrangements , pp. 713-769
    • Lemieux, R.U.1
  • 38
    • 0019194038 scopus 로고
    • The recognition of maltodextrins by Escherichia coli
    • Ferenci, T. (1980). The recognition of maltodextrins by Escherichia coli. Eur. J. Biochem. 108, 631-636.
    • (1980) Eur. J. Biochem. , vol.108 , pp. 631-636
    • Ferenci, T.1
  • 39
    • 0021804775 scopus 로고
    • Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds
    • Pflugrath, J.W. & Quiocho, F.A. (1985). Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds. Nature 314, 257-260.
    • (1985) Nature , vol.314 , pp. 257-260
    • Pflugrath, J.W.1    Quiocho, F.A.2
  • 40
    • 0025000575 scopus 로고
    • High specificity of a phosphate transport protein determined by hydrogen bonds
    • Luecke, H. & Quiocho, F.A. (1990). High specificity of a phosphate transport protein determined by hydrogen bonds. Nature 347, 402-406.
    • (1990) Nature , vol.347 , pp. 402-406
    • Luecke, H.1    Quiocho, F.A.2
  • 41
    • 0024279631 scopus 로고
    • Sulfate-binding protein dislikes protonated oxyacids: A molecular explanation
    • Jacobson, B.L. & Quiocho, F.A. (1988). Sulfate-binding protein dislikes protonated oxyacids: a molecular explanation. J. Mol. Biol. 204, 783-787.
    • (1988) J. Mol. Biol. , vol.204 , pp. 783-787
    • Jacobson, B.L.1    Quiocho, F.A.2
  • 42
    • 0025217008 scopus 로고
    • Refined crystal structure of the phosphorylase-heptulose 2-phosphate-oligosaccharide-AMP complex
    • Johnson, L.N., Acharya, K.R., Joran, M.D. & McLaughlin, P.J. (1990). Refined crystal structure of the phosphorylase-heptulose 2-phosphate-oligosaccharide-AMP complex. J. Mol. Biol. 211, 645-661.
    • (1990) J. Mol. Biol. , vol.211 , pp. 645-661
    • Johnson, L.N.1    Acharya, K.R.2    Joran, M.D.3    McLaughlin, P.J.4
  • 43
    • 0028181134 scopus 로고
    • Crystal structures of soybean β-amylase reacted with β-maltose and maltal: Active site components and their apparent role in catalysis
    • Mikami, B., Degano, M., Hehre, E.J. & Sacchettini, J.C. (1993). Crystal structures of soybean β-amylase reacted with β-maltose and maltal: active site components and their apparent role in catalysis. Biochemistry 33, 7779-7787.
    • (1993) Biochemistry , vol.33 , pp. 7779-7787
    • Mikami, B.1    Degano, M.2    Hehre, E.J.3    Sacchettini, J.C.4
  • 44
    • 0000289565 scopus 로고
    • The crystal and molecular structure of α-maltose
    • Takusagawa, F. & Jacobson, R.A. (1978). The crystal and molecular structure of α-maltose. Acta. Cryst. B 34, 213-218.
    • (1978) Acta. Cryst. B , vol.34 , pp. 213-218
    • Takusagawa, F.1    Jacobson, R.A.2
  • 45
    • 0001751718 scopus 로고
    • Regular left-handed fragment of amylose: Crystal and molecular structure of methyl-α-maltotrioside
    • Pangborn, W., Langs, D. & Perez, S. (1985). Regular left-handed fragment of amylose: crystal and molecular structure of methyl-α-maltotrioside. Int. J. Biol. Macromol. 7, 363-369.
    • (1985) Int. J. Biol. Macromol. , vol.7 , pp. 363-369
    • Pangborn, W.1    Langs, D.2    Perez, S.3
  • 46
    • 0025273178 scopus 로고
    • LamB (maltoporin) of Salmonella typhimurium: Isolation, purification a comparison of sugar binding with LamB of Escherichia coll
    • Schülein, K. & Benz, R. (1990). LamB (maltoporin) of Salmonella typhimurium: isolation, purification a comparison of sugar binding with LamB of Escherichia coll. Mol. Microbiol. 4, 625-362.
    • (1990) Mol. Microbiol. , vol.4 , pp. 625-1362
    • Schülein, K.1    Benz, R.2
  • 47
    • 0030033422 scopus 로고    scopus 로고
    • Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor
    • Yao, N., Ledvina, P.S., Choudhary, A. & Quiocho, F.A. (1996). Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor. Biochemistry 35, 2079-2085.
    • (1996) Biochemistry , vol.35 , pp. 2079-2085
    • Yao, N.1    Ledvina, P.S.2    Choudhary, A.3    Quiocho, F.A.4
  • 48
    • 0025145011 scopus 로고
    • Progress in the identification of interaction sites on the periplasmic maltose binding protein from E. coli
    • Martineau, P., Szmelcman, S., Hofnung, M., Spurlino, J.C. & Quiocho, F.A. (1990). Progress in the identification of interaction sites on the periplasmic maltose binding protein from E. coli. Biochimie 72, 397-402.
    • (1990) Biochimie , vol.72 , pp. 397-402
    • Martineau, P.1    Szmelcman, S.2    Hofnung, M.3    Spurlino, J.C.4    Quiocho, F.A.5
  • 49
    • 0017622429 scopus 로고
    • The 2.8-Å resolution structure of the L-arabinose-binding protein from Escherichia coli
    • Quiocho, F.A., Gilliland, G.L. & Phillips, G.N.Jr. (1977). The 2.8-Å resolution structure of the L-arabinose-binding protein from Escherichia coli. J. Biol. Chem. 252, 5142-5149.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5142-5149
    • Quiocho, F.A.1    Gilliland, G.L.2    Phillips Jr., G.N.3
  • 50
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W.A. (1985). Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 51
    • 0000082544 scopus 로고
    • CHAIN - A crystallographic modeling program
    • Sack, J.S. (1988). CHAIN - a crystallographic modeling program. J. Mol. Graph. 6, 244-245.
    • (1988) J. Mol. Graph. , vol.6 , pp. 244-245
    • Sack, J.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.