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Volumn 44, Issue 13, 2005, Pages 5053-5064

Direct evidence for Sphingomonas sp. A1 periplasmic proteins as macromolecule-binding proteins associated with the ABC transporter: Molecular insights into alginate transport in the periplasm

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BACTERIA; BIOSENSORS; MACROMOLECULES; POLYMERIZATION; RESONANCE; SPECTROSCOPY; X RAY CRYSTALLOGRAPHY;

EID: 16344366722     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047781r     Document Type: Article
Times cited : (38)

References (33)
  • 2
    • 0033759340 scopus 로고    scopus 로고
    • Alginate lyase: Review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications
    • Wong, T. Y., Preston, L. A., and Schiller, N. L. (2000) Alginate lyase: Review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications, Annu. Rev. Microbiol. 54, 289-340.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 289-340
    • Wong, T.Y.1    Preston, L.A.2    Schiller, N.L.3
  • 3
    • 0029159895 scopus 로고
    • Direct uptake of alginate molecules through a pit on the bacterial cell surface: A novel mechanism for the uptake of macromolecules
    • Hisano, T., Yonemoto, Y., Yamashita, T., Fukuda, Y., Kimura, A., and Murata, K. (1995) Direct uptake of alginate molecules through a pit on the bacterial cell surface: A novel mechanism for the uptake of macromolecules, J. Ferment. Bioeng. 79, 538-544.
    • (1995) J. Ferment. Bioeng. , vol.79 , pp. 538-544
    • Hisano, T.1    Yonemoto, Y.2    Yamashita, T.3    Fukuda, Y.4    Kimura, A.5    Murata, K.6
  • 5
    • 0033932250 scopus 로고    scopus 로고
    • A novel bacterial ATP-binding cassette (ABC) transporter system that allows uptake of macromolecules
    • Momma, K., Okamoto, M., Mishima, Y., Mori, S., Hashimoto, W., and Murata, K. (2000) A novel bacterial ATP-binding cassette (ABC) transporter system that allows uptake of macromolecules, J. Bacteriol. 182, 3998-4004.
    • (2000) J. Bacteriol. , vol.182 , pp. 3998-4004
    • Momma, K.1    Okamoto, M.2    Mishima, Y.3    Mori, S.4    Hashimoto, W.5    Murata, K.6
  • 6
    • 0034084571 scopus 로고    scopus 로고
    • Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases
    • Yoon, H.-J., Hashimoto, W., Miyake, O., Okamoto, M., Mikami, B., and Murata, K. (2000) Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases, Protein Expression Purif. 19, 84-90.
    • (2000) Protein Expression Purif. , vol.19 , pp. 84-90
    • Yoon, H.-J.1    Hashimoto, W.2    Miyake, O.3    Okamoto, M.4    Mikami, B.5    Murata, K.6
  • 7
    • 0033905713 scopus 로고    scopus 로고
    • Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate
    • Hashimoto, W., Miyake, O., Momma, K., Kawai, S., and Murata, K. (2000) Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as one of the enzymes required for complete depolymerization of alginate, J. Bacteriol. 182, 4572-4577.
    • (2000) J. Bacteriol. , vol.182 , pp. 4572-4577
    • Hashimoto, W.1    Miyake, O.2    Momma, K.3    Kawai, S.4    Murata, K.5
  • 8
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A. L., and Chen, J. (2004) ATP-binding cassette transporters in bacteria, Annu. Rev. Biochem. 73, 241-268.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 9
    • 0031943304 scopus 로고    scopus 로고
    • The Escherichia coli ATP-binding cassette (ABC) proteins
    • Linton, K. J., and Higgins, C. F. (1998) The Escherichia coli ATP-binding cassette (ABC) proteins, Mol. Microbiol. 28, 5-13.
    • (1998) Mol. Microbiol. , vol.28 , pp. 5-13
    • Linton, K.J.1    Higgins, C.F.2
  • 10
    • 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
  • 11
    • 0036304144 scopus 로고    scopus 로고
    • Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. A1 at 2.0 Å resolution
    • Momma, K., Mikami, B., Mishima, Y., Hashimoto, W., and Murata, K. (2002) Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. A1 at 2.0 Å resolution, J. Mol. Biol. 316, 1061-1069.
    • (2002) J. Mol. Biol. , vol.316 , pp. 1061-1069
    • Momma, K.1    Mikami, B.2    Mishima, Y.3    Hashimoto, W.4    Murata, K.5
  • 12
    • 0037458573 scopus 로고    scopus 로고
    • Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. A1, complexed with an alginate tetrasaccharide at 1.6-Å resolution
    • Mishima, Y., Momma, K., Hashimoto, W., Mikami, B., and Murata, K. (2003) Crystal structure of AlgQ2, a macromolecule (alginate)-binding protein of Sphingomonas sp. A1, complexed with an alginate tetrasaccharide at 1.6-Å resolution, J. Biol. Chem. 278, 6552-6559.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6552-6559
    • Mishima, Y.1    Momma, K.2    Hashimoto, W.3    Mikami, B.4    Murata, K.5
  • 14
    • 0016439201 scopus 로고
    • Isolation and characterization of two outer membrane preparations from Escherichia coli
    • Mizushima, S., and Yamada, H. (1975) Isolation and characterization of two outer membrane preparations from Escherichia coli, Biochim. Biophys. Acta 375, 44-53.
    • (1975) Biochim. Biophys. Acta , vol.375 , pp. 44-53
    • Mizushima, S.1    Yamada, H.2
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0029123664 scopus 로고
    • Effect of site-directed mutations on processing and activity of γ-glutamyltranspeptidase of Escherichia coli K-12
    • Hashimoto, W., Suzuki, H., Yamamoto, K., and Kumagai, H. (1995) Effect of site-directed mutations on processing and activity of γ- glutamyltranspeptidase of Escherichia coli K-12, J. Biochem. 118, 75-80.
    • (1995) J. Biochem. , vol.118 , pp. 75-80
    • Hashimoto, W.1    Suzuki, H.2    Yamamoto, K.3    Kumagai, H.4
  • 19
    • 0031783859 scopus 로고    scopus 로고
    • Sphingomonas sp. A1 lyase active on both poly-β-D-mannuronate and heteropolymeric regions in alginate
    • Hashimoto, W., Okamoto, M., Hisano, T., Momma, K., and Murata, K. (1998) Sphingomonas sp. A1 lyase active on both poly-β-D-mannuronate and heteropolymeric regions in alginate, J. Ferment. Bioeng. 86, 236-238.
    • (1998) J. Ferment. Bioeng. , vol.86 , pp. 236-238
    • Hashimoto, W.1    Okamoto, M.2    Hisano, T.3    Momma, K.4    Murata, K.5
  • 20
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J. W. (1999) The finer things in X-ray diffraction data collection, Acta Crystallogr. D55, 1718-1725.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4 (1994) The CCP4 suite: Programs for protein crystallography, Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis, P. J. (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 26
    • 0028057108 scopus 로고
    • RASTER3D Version 2.0: A program for photorealistic molecular graphics
    • Merrit, E. A., and Murphy, M. E. P. (1994) RASTER3D Version 2.0: A program for photorealistic molecular graphics, Acta Crystallogr. D50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 27
  • 28
    • 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., and 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
  • 29
    • 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. U.S.A. 89, 2360-2364.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2360-2364
    • Davidson, A.L.1    Shuman, H.A.2    Nikaido, H.3
  • 30
    • 3142619074 scopus 로고    scopus 로고
    • Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport
    • Austermuhle, M. I., Hall, J. A., Klug, C. S., and Davidson, A. L. (2004) Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport, J. Biol. Chem. 279, 28243-28250.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28243-28250
    • Austermuhle, M.I.1    Hall, J.A.2    Klug, C.S.3    Davidson, A.L.4
  • 31
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design
    • Liang, J., Edelsbrunner, H., and Woodward, C. (1998) Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design, Protein Sci. 7, 1884-1897.
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3
  • 32
    • 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


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