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Volumn 4, Issue 2, 1996, Pages 127-134

Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway

Author keywords

Guided diffusion; LamB; Maltodextrin; Membrane protein; X ray structure

Indexed keywords

LAMBDA PHAGE RECEPTOR; MALTOOLIGOSACCHARIDES; OLIGOSACCHARIDE; VIRUS RECEPTOR;

EID: 0029644059     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00016-0     Document Type: Article
Times cited : (161)

References (34)
  • 1
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H. & Vaara, M. (1985). Molecular basis of bacterial outer membrane permeability. Microbiol. rev. 49, 1-32,
    • (1985) Microbiol. Rev. , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 2
    • 0026538553 scopus 로고
    • Porins and specific channels of bacterial outer membranes
    • Nikaido, H. (1992). Porins and specific channels of bacterial outer membranes. Mol. Microbiol. 6, 435-442.
    • (1992) Mol. Microbiol. , vol.6 , pp. 435-442
    • Nikaido, H.1
  • 3
    • 0018703721 scopus 로고
    • E. coli mutants impaired in maltodextrin transport
    • Wandersman, C., Schwartz, M. & Ferenci, T. (1979). E. coli mutants impaired in maltodextrin transport. J. Bacteriol. 140, 1-13.
    • (1979) J. Bacteriol. , vol.140 , pp. 1-13
    • Wandersman, C.1    Schwartz, M.2    Ferenci, T.3
  • 4
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution
    • Schirmer, T., Keller, T.A., Wang, Y.-F. & Rosenbusch, J.P. (1995). Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution. Science 267, 512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.-F.3    Rosenbusch, J.P.4
  • 5
    • 0018826901 scopus 로고
    • The permeability of the endplate channel to organic cations in frog muscle
    • Dwyer, T.M., Adams, D.J. & Hille, B. (1980). The permeability of the endplate channel to organic cations in frog muscle. J. Gen. Physiol. 75, 469-492.
    • (1980) J. Gen. Physiol. , vol.75 , pp. 469-492
    • Dwyer, T.M.1    Adams, D.J.2    Hille, B.3
  • 6
    • 0009551491 scopus 로고
    • Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli
    • Luckey, M. & Nikaido, H. (1980). Specificity of diffusion channels produced by lambda phage receptor protein of Escherichia coli. Proc. Natl. Acad. Sci. USA 77, 167-171.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 167-171
    • Luckey, M.1    Nikaido, H.2
  • 7
    • 0023698816 scopus 로고
    • Mutations that alter the pore function of the OmpF porin of Escherichia coli K12
    • Benson, S.A., Occi, J.L.L. & Sampson, B.A. (1988). Mutations that alter the pore function of the OmpF porin of Escherichia coli K12. J. Mol. Biol. 203, 961-970.
    • (1988) J. Mol. Biol. , vol.203 , pp. 961-970
    • Benson, S.A.1    Occi, J.L.L.2    Sampson, B.A.3
  • 8
    • 0022515322 scopus 로고
    • Pore formation by LamB of Escherichia coli in lipid bilayer membranes
    • Benz, R., Schmid, A., Nakae, T. & Vos-Scherperkeuter, G.H. (1986). Pore formation by LamB of Escherichia coli in lipid bilayer membranes. J. Bacteriol. 165, 978-986.
    • (1986) J. Bacteriol. , vol.165 , pp. 978-986
    • Benz, R.1    Schmid, A.2    Nakae, T.3    Vos-Scherperkeuter, G.H.4
  • 9
    • 0023472905 scopus 로고
    • Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane
    • Benz, R., Schmid, A., Greetje, H. & Vos-Scheperkeuter, H. (1987). Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane. J. Membr. Biol. 100, 21-29.
    • (1987) J. Membr. Biol. , vol.100 , pp. 21-29
    • Benz, R.1    Schmid, A.2    Greetje, H.3    Vos-Scheperkeuter, H.4
  • 10
    • 0023650005 scopus 로고
    • Selectivity for maltose and maltodextrins of maltoporin, a pore-forming protein of E.coli outer membrane
    • Dargent, B., Rosenbusch, J.P. & Pattus, F. (1987). Selectivity for maltose and maltodextrins of maltoporin, a pore-forming protein of E.coli outer membrane. FEBS Lett. 220, 136-142.
    • (1987) FEBS Lett. , vol.220 , pp. 136-142
    • Dargent, B.1    Rosenbusch, J.P.2    Pattus, F.3
  • 11
    • 0026064182 scopus 로고
    • Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from E.coli
    • Gehring, K., Cheng, C.-H., Nikaido, H. & Jap, B.K. (1991). Stoichiometry of maltodextrin-binding sites in LamB, an outer membrane protein from E.coli. J. Bacteriol. 173, 1873-1878.
    • (1991) J. Bacteriol. , vol.173 , pp. 1873-1878
    • Gehring, K.1    Cheng, C.-H.2    Nikaido, H.3    Jap, B.K.4
  • 12
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E. coli porins
    • Cowan, S.W., et al., & Rosenbusch, J.P. (1992). Crystal structures explain functional properties of two E. coli porins. Nature 358, 727-733.
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Rosenbusch, J.P.2
  • 13
    • 0026737314 scopus 로고
    • Structure of porin refined at 1.8 Å resolution
    • Weiss, M.S. & Schulz, G.E. (1992). Structure of porin refined at 1.8 Å resolution. J. Mol. Biol. 227, 493-509.
    • (1992) J. Mol. Biol. , vol.227 , pp. 493-509
    • Weiss, M.S.1    Schulz, G.E.2
  • 14
    • 0027457784 scopus 로고
    • Derepression of LamB protein facilitates outer membrane permeation of carbohydrates into Escherichia coli under conditions of nutrient stress
    • Death, A., Notley, L. & Ferenci, T. (1993). Derepression of LamB protein facilitates outer membrane permeation of carbohydrates into Escherichia coli under conditions of nutrient stress. J. Bacteriol. 175, 1475-1483.
    • (1993) J. Bacteriol. , vol.175 , pp. 1475-1483
    • Death, A.1    Notley, L.2    Ferenci, T.3
  • 15
    • 0020056622 scopus 로고
    • Structure of maltoheptaose by Difference Fourier methods and a model of glycogen
    • Goldsmith, E., Sprang, S. & Flettrick, R. (1982). Structure of maltoheptaose by Difference Fourier methods and a model of glycogen. J. Mol. Biol. 156, 411-427.
    • (1982) J. Mol. Biol. , vol.156 , pp. 411-427
    • Goldsmith, E.1    Sprang, S.2    Flettrick, R.3
  • 16
    • 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
  • 17
    • 0020491174 scopus 로고
    • Directed evolution of the lambda receptor of Escherichia coli through affinity Chromatographic selection
    • Ferenci, T. & Lee, K.-S. (1982). Directed evolution of the lambda receptor of Escherichia coli through affinity Chromatographic selection. J. Mol. Biol. 160, 431-444.
    • (1982) J. Mol. Biol. , vol.160 , pp. 431-444
    • Ferenci, T.1    Lee, K.-S.2
  • 18
    • 0023193694 scopus 로고
    • Sequence determinants in the lamB gene of E. coli influencing the binding and pore selectivity of maltoporin
    • Heine, H.G., Kyngdon, J. & Ferenci, T. (1987). Sequence determinants in the lamB gene of E. coli influencing the binding and pore selectivity of maltoporin. Gene 53, 287-292.
    • (1987) Gene , vol.53 , pp. 287-292
    • Heine, H.G.1    Kyngdon, J.2    Ferenci, T.3
  • 19
    • 0022615217 scopus 로고
    • The role of the maltodextrin-binding site in determining the transport properties of the LamB protein
    • Nakae, T., Ishii, J. & Ferenci, T. (1986). The role of the maltodextrin-binding site in determining the transport properties of the LamB protein. J. Biol. Chem. 261, 622-626.
    • (1986) J. Biol. Chem. , vol.261 , pp. 622-626
    • Nakae, T.1    Ishii, J.2    Ferenci, T.3
  • 20
    • 0026545214 scopus 로고
    • Investigation of the selectivity of maltoporin channels using mutant LamB proteins: Mutations changing the maltodextrin binding site
    • Benz, R., Francis, G., Nakae, T. & Ferenci, T. (1992). Investigation of the selectivity of maltoporin channels using mutant LamB proteins: mutations changing the maltodextrin binding site. Biochem. Biophys. Acta 1104, 299-307.
    • (1992) Biochem. Biophys. Acta , vol.1104 , pp. 299-307
    • Benz, R.1    Francis, G.2    Nakae, T.3    Ferenci, T.4
  • 21
    • 84982409240 scopus 로고
    • Selectivity in solute transport: Binding sites and channel structure in maltoporin and other bacterial sugar transport proteins
    • Ferenci, T. (1989). Selectivity in solute transport: Binding sites and channel structure in maltoporin and other bacterial sugar transport proteins. BioEssays 10, 3-7.
    • (1989) BioEssays , vol.10 , pp. 3-7
    • Ferenci, T.1
  • 22
    • 0018966820 scopus 로고
    • Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrins and starch polysaccharides
    • Ferenci, T., Schwentorat, M., Ullrich, S. & Vilmart, J. (1980). Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrins and starch polysaccharides. J. Bacteriol. 142, 521-526.
    • (1980) J. Bacteriol. , vol.142 , pp. 521-526
    • Ferenci, T.1    Schwentorat, M.2    Ullrich, S.3    Vilmart, J.4
  • 23
    • 0028926959 scopus 로고
    • Evaluation of the rate constants of sugar transport through maltoporin (LamB) of E coli from the sugar-induced current noise
    • Andersen, C., Jordy, M. & Benz, R. (1995). Evaluation of the rate constants of sugar transport through maltoporin (LamB) of E coli from the sugar-induced current noise. J. Gen. Physiol. 105, 385-401.
    • (1995) J. Gen. Physiol. , vol.105 , pp. 385-401
    • Andersen, C.1    Jordy, M.2    Benz, R.3
  • 25
    • 0025322309 scopus 로고
    • Channels as Enzymes
    • Eisenberg, R.S. (1990). Channels as Enzymes. J. Membr Biol., 115, 1-12.
    • (1990) J. Membr Biol. , vol.115 , pp. 1-12
    • Eisenberg, R.S.1
  • 26
    • 0029012475 scopus 로고
    • Pore loops: An emerging theme in ion channel structure
    • MacKinnon, R. (1995). Pore loops: an emerging theme in ion channel structure. Neuron 14, 889-892.
    • (1995) Neuron , vol.14 , pp. 889-892
    • MacKinnon, R.1
  • 27
    • 0028275219 scopus 로고
    • Crystallization of monodisperse maltoporin from wild-type and mutant strains of various Enterobacteriaceae
    • Keller, T.A., Ferenci, T., Prilipov, A. & Rosenbusch, J.P. (1994). Crystallization of monodisperse maltoporin from wild-type and mutant strains of various Enterobacteriaceae. Bioch. Biophys. Res. Commun. 199, 767-771.
    • (1994) Bioch. Biophys. Res. Commun. , vol.199 , pp. 767-771
    • Keller, T.A.1    Ferenci, T.2    Prilipov, A.3    Rosenbusch, J.P.4
  • 28
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993). Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystal. 26, 795-800.
    • (1993) J. Appl. Crystal. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 29
    • 0003195664 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • SERC Daresbury Laboratory, Warrington, UK
    • Leslie, A.G.W. (1991). Recent changes to the MOSFLM package for processing film and image plate data. In Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography. SERC Daresbury Laboratory, Warrington, UK.
    • (1991) Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography
    • Leslie, A.G.W.1
  • 30
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 32
    • 0002700643 scopus 로고
    • Halloween... masks and bones
    • (Bailey, S., Hubbard, R. & Waller, D. eds), SERC Daresbury Laboratory, Daresbury, UK
    • Kleywegt, G.J. & Jones, T.A. (1994). Halloween... masks and bones. In Proceedings of the CCP4 study weekend: From first map to final model, (Bailey, S., Hubbard, R. & Waller, D. eds), pp. 59-66, SERC Daresbury Laboratory, Daresbury, UK.
    • (1994) Proceedings of the CCP4 Study Weekend: from First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystal. 24, 946-950.
    • (1991) J. Appl. Crystal. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.