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Volumn 68, Issue 3, 2007, Pages 796-801

Crystal structure of a cyanobacterial sucrose-phosphatase in complex with glucose-containing disaccharides

Author keywords

[No Author keywords available]

Indexed keywords

CELLOBIOSE; DISACCHARIDE; GLUCOSE; MALTOSE; PHOSPHATASE; SUCROSE; SUCROSE PHOSPHATASE; TREHALOSE; UNCLASSIFIED DRUG;

EID: 34447511603     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21481     Document Type: Article
Times cited : (7)

References (26)
  • 1
    • 0000665346 scopus 로고
    • The biosynthesis of sucrose phosphate
    • Leloir LF, Cardini CE. The biosynthesis of sucrose phosphate. J Biol Chem 1955;214:157-165.
    • (1955) J Biol Chem , vol.214 , pp. 157-165
    • Leloir, L.F.1    Cardini, C.E.2
  • 2
    • 0013894039 scopus 로고
    • A specific sucrose phosphatase from plant tissues
    • Hawker JS, Hatch MD. A specific sucrose phosphatase from plant tissues. Biochem J 1966;99:102-107.
    • (1966) Biochem J , vol.99 , pp. 102-107
    • Hawker, J.S.1    Hatch, M.D.2
  • 3
    • 0033740573 scopus 로고    scopus 로고
    • Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants
    • Lunn JE, Ashton AR, Hatch MD, Heldt HW. Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants. Proc Natl Acad Sci USA 2000;97:12914-12919.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12914-12919
    • Lunn, J.E.1    Ashton, A.R.2    Hatch, M.D.3    Heldt, H.W.4
  • 4
    • 0036010499 scopus 로고    scopus 로고
    • Evolution of sucrose synthesis
    • Lunn JE. Evolution of sucrose synthesis. Plant Physiol 2002;128: 1490-1500.
    • (2002) Plant Physiol , vol.128 , pp. 1490-1500
    • Lunn, J.E.1
  • 5
    • 33644798734 scopus 로고    scopus 로고
    • The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell
    • Fieulaine S, Lunn JE, Borel F, Ferrer JL. The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell. Plant Cell 2005;17:2049-2058.
    • (2005) Plant Cell , vol.17 , pp. 2049-2058
    • Fieulaine, S.1    Lunn, J.E.2    Borel, F.3    Ferrer, J.L.4
  • 6
    • 21344466538 scopus 로고    scopus 로고
    • Decreased sucrose-6-phosphate phosphatase level in transgenic tobacco inhibits photosynthesis, alters carbohydrate partitioning, and reduces growth
    • Chen S, Hajirezaei M, Peisker M, Tschiersch H, Sonnewald U, Börnke F. Decreased sucrose-6-phosphate phosphatase level in transgenic tobacco inhibits photosynthesis, alters carbohydrate partitioning, and reduces growth. Planta 2005;221:479-492.
    • (2005) Planta , vol.221 , pp. 479-492
    • Chen, S.1    Hajirezaei, M.2    Peisker, M.3    Tschiersch, H.4    Sonnewald, U.5    Börnke, F.6
  • 7
    • 0000760288 scopus 로고
    • Occurrence of sucrose phosphatase in vascular and non-vascular plants
    • Hawker JS, Smith GM. Occurrence of sucrose phosphatase in vascular and non-vascular plants. Phytochemistry 1984;23:245-249.
    • (1984) Phytochemistry , vol.23 , pp. 245-249
    • Hawker, J.S.1    Smith, G.M.2
  • 8
    • 0001736888 scopus 로고
    • Purification and properties of sucrose-6-phosphatase from Pisum sativum shoots
    • Whitaker DP. Purification and properties of sucrose-6-phosphatase from Pisum sativum shoots. Phytochemistry 1984;23:2429-2430.
    • (1984) Phytochemistry , vol.23 , pp. 2429-2430
    • Whitaker, D.P.1
  • 9
    • 0028065910 scopus 로고
    • Properties of sucrose-phosphate phosphatase from rice (Oryza sativa) leaves
    • Echeverria E, Salerno G. Properties of sucrose-phosphate phosphatase from rice (Oryza sativa) leaves. Plant Sci 1994;96:15-19.
    • (1994) Plant Sci , vol.96 , pp. 15-19
    • Echeverria, E.1    Salerno, G.2
  • 10
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 1993;26:795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 12
    • 34447500416 scopus 로고    scopus 로고
    • Roussel A, Cambillau C. TURBO-FRODO. In: Silicon graphics geometry partners directory. Mountain View, CA: Silicon Graphics; 1989, pp. 77-78.
    • Roussel A, Cambillau C. TURBO-FRODO. In: Silicon graphics geometry partners directory. Mountain View, CA: Silicon Graphics; 1989, pp. 77-78.
  • 13
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf RM. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph Model 1997;15:112-134.
    • (1997) J Mol Graph Model , vol.15 , pp. 112-134
    • Esnouf, R.M.1
  • 14
    • 0033119938 scopus 로고    scopus 로고
    • Esnouf RM. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr Sect D. Biol Crystallogr 1999;55 (Pt 4):938-940
    • Esnouf RM. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr Sect D. Biol Crystallogr 1999;55 (Pt 4):938-940.
  • 15
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt EA, Bacon DJ. Raster3D: photorealistic molecular graphics. Methods Enzymol 1997;277:505-524.
    • (1997) Methods Enzymol , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 16
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones G, Willett P, Glen RC. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J Mol Biol 1995;245:43-53.
    • (1995) J Mol Biol , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 18
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 19
    • 20544469463 scopus 로고    scopus 로고
    • HAD superfamily phosphotransferase substrate diversification: Structure and function analysis of HAD subclass IIB sugar phosphatase BT4131
    • Lu Z, Dunaway-Mariano D, Allen KN. HAD superfamily phosphotransferase substrate diversification: structure and function analysis of HAD subclass IIB sugar phosphatase BT4131. Biochemistry 2005; 44:8684-8696.
    • (2005) Biochemistry , vol.44 , pp. 8684-8696
    • Lu, Z.1    Dunaway-Mariano, D.2    Allen, K.N.3
  • 21
    • 0024237631 scopus 로고
    • Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein
    • Vyas NK, Vyas MN, Quiocho FA. Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein. Science 1988;242:1290-1295.
    • (1988) Science , vol.242 , pp. 1290-1295
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 22
    • 12944260514 scopus 로고
    • Atomic features of protein-carbohydrate interactions
    • Vyas NK. Atomic features of protein-carbohydrate interactions. Curr Opin Struct Biol 1991;1:732-740.
    • (1991) Curr Opin Struct Biol , vol.1 , pp. 732-740
    • Vyas, N.K.1
  • 23
    • 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 JA, Nikaido H, Quiocho FA. Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding. J Mol Biol 2001;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
  • 24
    • 13844312649 scopus 로고    scopus 로고
    • ZINC - a free database of commercially available compounds for virtual screening
    • Irwin JJ, Shoichet BK. ZINC - a free database of commercially available compounds for virtual screening. J Chem Inf Model 2005;45:177-182.
    • (2005) J Chem Inf Model , vol.45 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 25
    • 0033136352 scopus 로고    scopus 로고
    • Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803
    • Lunn JE, Price GD, Furbank RT. Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol Biol 1999;40:297-305.
    • (1999) Plant Mol Biol , vol.40 , pp. 297-305
    • Lunn, J.E.1    Price, G.D.2    Furbank, R.T.3
  • 26
    • 33746922036 scopus 로고    scopus 로고
    • Evolutionary genomics of the HAD superfamily: Understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes
    • Burroughs AM, Allen KN, Dunaway-Mariano D, Aravind L. Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes. J Mol Biol 2006;361:1003-1034.
    • (2006) J Mol Biol , vol.361 , pp. 1003-1034
    • Burroughs, A.M.1    Allen, K.N.2    Dunaway-Mariano, D.3    Aravind, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.