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Volumn 57, Issue SUPPL. 11, 2002, Pages 109-118

A structural model for the N-terminal N1 module of E. coli glycogen branching enzyme

Author keywords

amylase family; Domain duplication; Glycogen branching enzyme; Homology model; N domain; Structure

Indexed keywords

ESCHERICHIA COLI; PROKARYOTA; PSEUDOMONAS; PSEUDOMONAS AMYLODERAMOSA; SULFOLOBUS; SULFOLOBUS SOLFATARICUS;

EID: 0346997318     PISSN: 13356399     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (12)

References (49)
  • 4
    • 0023025007 scopus 로고
    • Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase as deduced from the nucleotide sequence of the glg B gene
    • BAECKER, P. A., GREENBERG, E. & PREISS, J. 1986. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli 1,4-α-D-glucan:1,4-α-D-glucan 6-α-D-(1,4-α-D-glucano)-transferase as deduced from the nucleotide sequence of the glg B gene. J. Biol. Chem. 261: 8738-8743.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8738-8743
    • Baecker, P.A.1    Greenberg, E.2    Preiss, J.3
  • 5
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • BARTON, G. J. 1993. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6: 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 6
    • 0034657390 scopus 로고    scopus 로고
    • Limited proteolysis of branching enzyme from Escherichia coli
    • BINDERUP, K., MIKKELSEN, R. & PREISS, J. 2000. Limited proteolysis of branching enzyme from Escherichia coli. Arch. Biochem. Biophys. 377: 366-371.
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 366-371
    • Binderup, K.1    Mikkelsen, R.2    Preiss, J.3
  • 8
    • 0028839801 scopus 로고
    • Tissue-specific glycogen branching isoenzymes in a multicellular prokaryote, Streptomyces coelicolor A3(2)
    • BRUTON, C. J., PLASKITT, K. A. & CHATER, K. F. 1995. Tissue-specific glycogen branching isoenzymes in a multicellular prokaryote, Streptomyces coelicolor A3(2). Mol. Microbiol. 18: 89-99.
    • (1995) Mol. Microbiol. , vol.18 , pp. 89-99
    • Bruton, C.J.1    Plaskitt, K.A.2    Chater, K.F.3
  • 9
    • 0343747835 scopus 로고    scopus 로고
    • Molecular cloning, functional expression and purification of a glucan branching enzyme from Neisseria denitrificans
    • BUETTCHER, V., QUANZ, M., & WILLMITZER, L. 1999. Molecular cloning, functional expression and purification of a glucan branching enzyme from Neisseria denitrificans. Biochim. Biophys. Acta 1432: 406-412.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 406-412
    • Buettcher, V.1    Quanz, M.2    Willmitzer, L.3
  • 10
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • COLE, S. T., BROSCH, R., PARKHILL, J., GARNIER, T., CHURCIIER, C., HARRIS, D., et al. & BARRELL, B. G. 1998. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churciier, C.5    Harris, D.6    Barrell, B.G.7
  • 11
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • GILBERT, H. J., DAVIES, G. J., HENRISSAT, B. & SVENSSON, B. (eds) The Royal Society of Chemistry, Cambridge
    • COUTINHO, P. M. & HENRISSAT, B. 1999. Carbohydrate-active enzymes: an integrated database approach, pp. 3-12. In: GILBERT, H. J., DAVIES, G. J., HENRISSAT, B. & SVENSSON, B. (eds) Recent Advances in Carbohydrate Bioengineering, The Royal Society of Chemistry, Cambridge.
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 13
    • 0029610660 scopus 로고
    • Crystal structure of the flavo-hemoglobin from Alcaligenes eutrophus at 1.75 Å resolution
    • ERMLER, U., SIDDIQUI, R. A., CRAMM, R. & FRIEDRICH, B. 1995. Crystal structure of the flavo-hemoglobin from Alcaligenes eutrophus at 1.75 Å resolution. EMBO J. 14: 6067-6077.
    • (1995) EMBO J. , vol.14 , pp. 6067-6077
    • Ermler, U.1    Siddiqui, R.A.2    Cramm, R.3    Friedrich, B.4
  • 15
    • 0033654768 scopus 로고    scopus 로고
    • Hybrid fold recognition: Combining sequence derived properties with evolutionary information
    • ALTMAN, R. B., LAUDERDALE, K., DUNKER, A. K., HUNTER, L. & KLEIN, T. E. (eds) Proceedings of the Pacific Symposium, World Scientific Publishing Co., Hawaii
    • FISCHER, D. 2000. Hybrid fold recognition: combining sequence derived properties with evolutionary information, pp. 119-130. In: ALTMAN, R. B., LAUDERDALE, K., DUNKER, A. K., HUNTER, L. & KLEIN, T. E. (eds) Biocomputing 2000. Proceedings of the Pacific Symposium, World Scientific Publishing Co., Hawaii.
    • (2000) Biocomputing 2000 , pp. 119-130
    • Fischer, D.1
  • 17
    • 0034052144 scopus 로고    scopus 로고
    • Characterization and crystallization of an active N-terminally truncated form of the Escherichia coli glycogen branching enzyme
    • HILDEN, I., LO LEGGIO, L., LARSEN, S. & POULSEN, P. 2000. Characterization and crystallization of an active N-terminally truncated form of the Escherichia coli glycogen branching enzyme. Eur. J. Biochem. 267: 2150-2155.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2150-2155
    • Hilden, I.1    Lo Leggio, L.2    Larsen, S.3    Poulsen, P.4
  • 18
    • 0027958795 scopus 로고
    • Cloning of the putative glucogen branching enzyme gene, glgB, from Streptomyces aureofaciens
    • HOMEROVA, D. & KORMANEC, J. 1994. Cloning of the putative glucogen branching enzyme gene, glgB, from Streptomyces aureofaciens. Biochim. Biophys. Acta 1200: 334-336.
    • (1994) Biochim. Biophys. Acta , vol.1200 , pp. 334-336
    • Homerova, D.1    Kormanec, J.2
  • 20
    • 0027740009 scopus 로고
    • Starch-and glycogen-debranching and branching enzymes: Prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes
    • JESPERSEN, H. M., MACGREGOR, E. A., HENRISSAT, B., SIERKS, M. R. & SVENSSON, B. 1993. Starch-and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes. J. Protein Chem. 12: 791-805.
    • (1993) J. Protein Chem. , vol.12 , pp. 791-805
    • Jespersen, H.M.1    Macgregor, E.A.2    Henrissat, B.3    Sierks, M.R.4    Svensson, B.5
  • 21
    • 0026040317 scopus 로고
    • Comparison of the domain-level organization of starch hydrolases and related enzymes
    • JESPERSEN, H. M., MACGREGOR, E. A., SIERKS, M. R. & SVENSSON, B. 1991. Comparison of the domain-level organization of starch hydrolases and related enzymes. Biochem. J. 280: 51-55.
    • (1991) Biochem. J. , vol.280 , pp. 51-55
    • Jespersen, H.M.1    Macgregor, E.A.2    Sierks, M.R.3    Svensson, B.4
  • 22
    • 0033119569 scopus 로고    scopus 로고
    • A minor form of starch branching enzyme in potato (Solanum tuberosum L.) tubers has a major effect on starch structure: Cloning and characterisation of multiple forms of SBE A
    • JOBLING, S. A., SCHWALL, G. P., WESTCOTT, R. J., SIDEBOTTOM, C. M., DEBET, M., GIDLEY, M. J., JEFFCOAT, R. & SAFFORD, R. 1999. A minor form of starch branching enzyme in potato (Solanum tuberosum L.) tubers has a major effect on starch structure: cloning and characterisation of multiple forms of SBE A. Plant J. 18: 163-171.
    • (1999) Plant J. , vol.18 , pp. 163-171
    • Jobling, S.A.1    Schwall, G.P.2    Westcott, R.J.3    Sidebottom, C.M.4    Debet, M.5    Gidley, M.J.6    Jeffcoat, R.7    Safford, R.8
  • 23
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • JONES, D. T. 1999. GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J. Mol. Biol. 287: 797-815.
    • (1999) J. Mol. Biol. , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 24
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • JONES, T. A., ZOU, J. Y., COWAN, S. W. & KJELDGAARD, M. 1991. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47: 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 25
    • 0029655167 scopus 로고
    • Sequence analysis of the genome of the unicellular cyano-bacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome
    • KANEKO, T., TANAKA, A., SATO, S., KOTANI, H., SAZUKA, T., MIYAJIMA, N., SUGIURA, M. & TABATA, S. 1995. Sequence analysis of the genome of the unicellular cyano-bacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome. DNA Res. 2: 153-166.
    • (1995) DNA Res. , vol.2 , pp. 153-166
    • Kaneko, T.1    Tanaka, A.2    Sato, S.3    Kotani, H.4    Sazuka, T.5    Miyajima, N.6    Sugiura, M.7    Tabata, S.8
  • 26
    • 0033574502 scopus 로고    scopus 로고
    • Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution
    • KAMITORI, S., KONDO, S., OKUYAMA, K., YOKOTA, T., SHIMURA, Y., TONOZUKA, T. & SAKANO, Y. 1999. Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 Å resolution. J. Mol. Biol. 287: 907-921.
    • (1999) J. Mol. Biol. , vol.287 , pp. 907-921
    • Kamitori, S.1    Kondo, S.2    Okuyama, K.3    Yokota, T.4    Shimura, Y.5    Tonozuka, T.6    Sakano, Y.7
  • 27
    • 0032483304 scopus 로고    scopus 로고
    • Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolution
    • KATSUYA, Y., MEZAKI, Y., KUBOTA, M. & MATSUURA, Y. 1998. Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolution. J. Mol. Biol. 281: 885-897.
    • (1998) J. Mol. Biol. , vol.281 , pp. 885-897
    • Katsuya, Y.1    Mezaki, Y.2    Kubota, M.3    Matsuura, Y.4
  • 28
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • KELLEY, L. A., MACCALLUM, R. M. & STERNBERG, M. J. 2000. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299: 499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    Maccallum, R.M.2    Sternberg, M.J.3
  • 29
    • 0025291251 scopus 로고
    • Nucleotide sequence of the Synechococcus sp. PCC7942 branching enzyme gene (glgB): Expression in Bacillus subtilis
    • KIEL, J. A., BOELS, J. M., BELDMAN, G. & VENEMA, G. 1990. Nucleotide sequence of the Synechococcus sp. PCC7942 branching enzyme gene (glgB): expression in Bacillus subtilis. Gene 89: 77-84.
    • (1990) Gene , vol.89 , pp. 77-84
    • Kiel, J.A.1    Boels, J.M.2    Beldman, G.3    Venema, G.4
  • 30
    • 0026068257 scopus 로고
    • Molecular cloning and nucleotide sequence of the glycogen branching enzyme gene (glgB) from Bacillus stearothermophilus and expression in Escherichia coli and Bacillus subtilis
    • KIEL, J. A., BOELS, J. M., BELDMAN, G. & VENEMA, G. 1991. Molecular cloning and nucleotide sequence of the glycogen branching enzyme gene (glgB) from Bacillus stearothermophilus and expression in Escherichia coli and Bacillus subtilis. Mol. Gen. Genet. 230: 136-144.
    • (1991) Mol. Gen. Genet. , vol.230 , pp. 136-144
    • Kiel, J.A.1    Boels, J.M.2    Beldman, G.3    Venema, G.4
  • 31
    • 0027023616 scopus 로고
    • The glgB gene from the thermophile Bacillus caldolyticus encodes a thermolabile branching enzyme
    • KIEL, J. A., BOELS, J. M., BELDMAN, G. & VENEMA, G. 1992. The glgB gene from the thermophile Bacillus caldolyticus encodes a thermolabile branching enzyme. DNA Seq. 3: 221-232.
    • (1992) DNA Seq. , vol.3 , pp. 221-232
    • Kiel, J.A.1    Boels, J.M.2    Beldman, G.3    Venema, G.4
  • 32
    • 0028174763 scopus 로고
    • Glycogen in Bacillus subtilis: Molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation
    • KIEL, J. A., BOELS, J. M., BELDMAN, G. & VENEMA, G. 1994. Glycogen in Bacillus subtilis: molecular characterization of an operon encoding enzymes involved in glycogen biosynthesis and degradation. Mol. Microbiol. 11: 203-218.
    • (1994) Mol. Microbiol. , vol.11 , pp. 203-218
    • Kiel, J.A.1    Boels, J.M.2    Beldman, G.3    Venema, G.4
  • 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. Cryst. 24: 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0000243829 scopus 로고
    • PROCHECK - a program to check the stereochemical quality of protein structures
    • LASKOWSKI, R. A., MOSS, D. S. & THORNTON, J. M. 1993. PROCHECK - a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26: 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 36
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • MACGREGOR, E. A., JANECEK, S. & SVENSSON, B. 2001. Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim. Biophys. Acta 1546: 1-20.
    • (2001) Biochim. Biophys. Acta , vol.1546 , pp. 1-20
    • Macgregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 38
    • 0033576611 scopus 로고    scopus 로고
    • Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana
    • LIN, X., KAUL, S., ROUNSLEY, S., SHEA, T. P., BENITO, M. I., TOWN, C. D. et al. & VENTER, J. C. 1999. Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana. Nature 402: 761-768.
    • (1999) Nature , vol.402 , pp. 761-768
    • Lin, X.1    Kaul, S.2    Rounsley, S.3    Shea, T.P.4    Benito, M.I.5    Town, C.D.6    Venter, J.C.7
  • 39
    • 0031693058 scopus 로고    scopus 로고
    • Cloning and characterization of a nuclear gene encoding a starch branching enzyme from the marine red alga Gracilaria gracilis
    • LLUISMA, A. O. & RAGAN, M. A. 1998. Cloning and characterization of a nuclear gene encoding a starch branching enzyme from the marine red alga Gracilaria gracilis. Curr. Genet. 34: 105-111.
    • (1998) Curr. Genet. , vol.34 , pp. 105-111
    • Lluisma, A.O.1    Ragan, M.A.2
  • 41
    • 0026319199 scopus 로고
    • Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons
    • NICHOLLS, A., SHARP, K. A. & HONIG, B. 1991. Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 42
    • 0348023556 scopus 로고    scopus 로고
    • Designing ADP-glucose pyrophosphorylase and branching enzyme to alter starch levels and structure
    • Lisbon, Portugal, Abstract number 20174
    • th FEBS Meeting, Lisbon, Portugal, Abstract number 20174.
    • (2001) th FEBS Meeting
    • Preiss, J.1    Ballicora, M.A.2    Binderup, K.3
  • 43
    • 0025786512 scopus 로고
    • Characterization of the Butyrivibrio fibrisolvens glgB gene, which encodes a glycogen-branching enzyme with starch-clearing activity
    • RUMBAK, E., RAWLINGS, D. E., LINDSEY, G. G. & WOODS, D. R. 1991. Characterization of the Butyrivibrio fibrisolvens glgB gene, which encodes a glycogen-branching enzyme with starch-clearing activity. J. Bacteriol. 173: 6732-6741.
    • (1991) J. Bacteriol. , vol.173 , pp. 6732-6741
    • Rumbak, E.1    Rawlings, D.E.2    Lindsey, G.G.3    Woods, D.R.4
  • 45
    • 0026724939 scopus 로고
    • Coordinate regulation of glycogen metabolism in the yeast Saccharomyces cerevisiae. Induction of glycogen branching enzyme
    • THON, V. J., VIGNERON-LESENS, C., MARIANNE-PEPIN, T., MONTREUIL, J., DECO, A., RACHEZ, C., BALL, S. G. & CANNON, J. F. 1992. Coordinate regulation of glycogen metabolism in the yeast Saccharomyces cerevisiae. Induction of glycogen branching enzyme. J. Biol. Chem. 267: 15224-15228.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15224-15228
    • Thon, V.J.1    Vigneron-Lesens, C.2    Marianne-Pepin, T.3    Montreuil, J.4    Deco, A.5    Rachez, C.6    Ball, S.G.7    Cannon, J.F.8
  • 46
    • 0027531831 scopus 로고
    • Isolation of human glycogen branching enzyme cD-NAs by screening complementation in yeast
    • THON, V. J., KHALIL, M. & CANNON, J. F. 1993. Isolation of human glycogen branching enzyme cD-NAs by screening complementation in yeast. J. Biol. Chem. 268: 7509-7513.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7509-7513
    • Thon, V.J.1    Khalil, M.2    Cannon, J.F.3
  • 47
    • 0032414480 scopus 로고    scopus 로고
    • Gene organization and transcription analysis of the Agrobacterium tumefaciens glycogen (gig) operon: Two transcripts for the single phosphoglucomutase gene
    • UGALDE, J. E., LEPEK, V., UTTARO, A., ESTRELLA, J., IGLESIAS, A. & UGALDE, R. A. 1998. Gene organization and transcription analysis of the Agrobacterium tumefaciens glycogen (gig) operon: two transcripts for the single phosphoglucomutase gene. J. Bacteriol. 180: 6557-6564.
    • (1998) J. Bacteriol. , vol.180 , pp. 6557-6564
    • Ugalde, J.E.1    Lepek, V.2    Uttaro, A.3    Estrella, J.4    Iglesias, A.5    Ugalde, R.A.6
  • 48
    • 0035258450 scopus 로고    scopus 로고
    • The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 α-amylases: Effects of domain N on activity, specificity, stability and dimerization
    • YOKOTA, T., TONOZUKA, T., KAMITORI, S. & SAKANO Y. 2001. The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 α-amylases: effects of domain N on activity, specificity, stability and dimerization. Biosci. Biotechnol. Biochem. 65: 401-408.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 401-408
    • Yokota, T.1    Tonozuka, T.2    Kamitori, S.3    Sakano, Y.4
  • 49
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • WATANABE, K., HATA, Y., KIZAKI, H., KATSUBE, Y. & SUZUKI, Y. 1997. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol. 269: 142-153.
    • (1997) J. Mol. Biol. , vol.269 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5


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