메뉴 건너뛰기




Volumn 17, Issue 7, 2005, Pages 2049-2058

The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOSYNTHESIS; CATALYSIS; CELLS; METABOLITES; SUGAR (SUCROSE);

EID: 33644798734     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.105.031229     Document Type: Article
Times cited : (53)

References (35)
  • 1
    • 0031970010 scopus 로고    scopus 로고
    • The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    • Aravind, L., Galperin, M.Y., and Koonin, E.V. (1998). The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem. Sci. 23, 127-129.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 127-129
    • Aravind, L.1    Galperin, M.Y.2    Koonin, E.V.3
  • 2
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T., et al. (1998). Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 3
    • 0032486282 scopus 로고    scopus 로고
    • A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif
    • Collet, J.-F., Stroobant, V., Pirard, M., Delpierre, G., and Van Schaftingen, E. (1998). A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif. J. Biol. Chem. 273, 14107-14112.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14107-14112
    • Collet, J.-F.1    Stroobant, V.2    Pirard, M.3    Delpierre, G.4    Van Schaftingen, E.5
  • 4
    • 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, J.A., Nikaido, H., and Quiocho, F.A. (2001). Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: Flexibility of tertiary structure and ligand binding. J. Mol. Biol. 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
  • 5
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. (1997). An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 112-113, 132-134.
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 112-113
    • Esnouf, R.M.1
  • 6
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R.M. (1999). Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D Biol. Crystallogr. 55, 938-940.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 7
    • 0036711227 scopus 로고    scopus 로고
    • Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase
    • Galburt, E.A., Pelletier, J., Wilson, G., and Stoddard, B.L. (2002). Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase. Structure 10, 1249-1260.
    • (2002) Structure , vol.10 , pp. 1249-1260
    • Galburt, E.A.1    Pelletier, J.2    Wilson, G.3    Stoddard, B.L.4
  • 8
    • 0013894039 scopus 로고
    • A specific sucrose phosphatase from plant tissues
    • Hawker, J.S., and Hatch, M.D. (1966). A specific sucrose phosphatase from plant tissues. Biochem. J. 99, 102-107.
    • (1966) Biochem. J. , vol.99 , pp. 102-107
    • Hawker, J.S.1    Hatch, M.D.2
  • 9
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm, L., and Sander, C. (1996). Mapping the protein universe. Science 273, 595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 10
    • 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. Crystallogr. 26, 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 13
    • 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
  • 14
    • 0037008092 scopus 로고    scopus 로고
    • Caught in the act: The structure of β-phosphoglucomutase from Lactococcus lactis
    • Lahiri, S.D., Zhang, G., Dunaway-Mariano, D., and Allen, K.N. (2002). Caught in the act: The structure of β-phosphoglucomutase from Lactococcus lactis. Biochemistry 41, 8351-8359.
    • (2002) Biochemistry , vol.41 , pp. 8351-8359
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 15
    • 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
  • 16
    • 0000665346 scopus 로고
    • The biosynthesis of sucrose phosphate
    • Leloir, L.F., and Cardini, C.E. (1955). The biosynthesis of sucrose phosphate. J. Biol. Chem. 214, 157-165.
    • (1955) J. Biol. Chem. , vol.214 , pp. 157-165
    • Leloir, L.F.1    Cardini, C.E.2
  • 17
    • 0036010499 scopus 로고    scopus 로고
    • Evolution of sucrose synthesis
    • Lunn, J.E. (2002). Evolution of sucrose synthesis. Plant Physiol. 129, 1490-1500.
    • (2002) Plant Physiol. , vol.129 , pp. 1490-1500
    • Lunn, J.E.1
  • 18
    • 0025271020 scopus 로고
    • Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of Pisum sativum
    • Lunn, J.E., and ap Rees, T. (1990a). Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of Pisum sativum. Biochem. J. 267, 739-743.
    • (1990) Biochem. J. , vol.267 , pp. 739-743
    • Lunn, J.E.1    Ap Rees, T.2
  • 19
    • 0001041359 scopus 로고
    • Purification and properties of sucrose-phosphate synthase from seeds of Pisum sativum
    • Lunn, J.E., and ap Rees, T. (1990b). Purification and properties of sucrose-phosphate synthase from seeds of Pisum sativum. Phytochem. 29, 1057-1063.
    • (1990) Phytochem. , vol.29 , pp. 1057-1063
    • Lunn, J.E.1    Ap Rees, T.2
  • 20
    • 0033740573 scopus 로고    scopus 로고
    • Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants
    • Lunn, J.E., Ashton, A.R., Hatch, M.D., and Heldt, H.W. (2000). Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants. Proc. Natl. Acad. Sci. USA 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
  • 21
    • 0033136352 scopus 로고    scopus 로고
    • Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803
    • Lunn, J.E., Price, G.D., and Furbank, R.T. (1999). Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol. Biol. 40, 297-305.
    • (1999) Plant Mol. Biol. , vol.40 , pp. 297-305
    • Lunn, J.E.1    Price, G.D.2    Furbank, R.T.3
  • 22
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A., and Bacon, D.J. (1997). Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 23
    • 0034730072 scopus 로고    scopus 로고
    • The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: Insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily
    • Morais, M.C., Zhang, W., Baker, A.S., Zhang, G., Dunaway-Mariano, D., and Allen, K.N. (2000). The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: Insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Biochemistry 39, 10385-10396.
    • (2000) Biochemistry , vol.39 , pp. 10385-10396
    • Morais, M.C.1    Zhang, W.2    Baker, A.S.3    Zhang, G.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 24
    • 0036499628 scopus 로고    scopus 로고
    • From structure to function: Yrbl from Haemophilus influenzae (HI1679) is a phosphatase
    • Parsons, J.F., Lim, K., Tempczyk, A., Krajewski, W., Eisenstein, E., and Herzberg, O. (2002). From structure to function: Yrbl from Haemophilus influenzae (HI1679) is a phosphatase. Proteins 46, 393-404.
    • (2002) Proteins , vol.46 , pp. 393-404
    • Parsons, J.F.1    Lim, K.2    Tempczyk, A.3    Krajewski, W.4    Eisenstein, E.5    Herzberg, O.6
  • 25
    • 0031455377 scopus 로고    scopus 로고
    • Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate
    • Ridder, I.S., Rozeboom, H.J., Kalk, K.H., Janssen, D.B., and Dijkstra, B.W. (1997). Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate. J. Biol. Chem. 272, 33015-33022.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33015-33022
    • Ridder, I.S.1    Rozeboom, H.J.2    Kalk, K.H.3    Janssen, D.B.4    Dijkstra, B.W.5
  • 28
    • 0037633997 scopus 로고    scopus 로고
    • Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima
    • Shin, D.H., Roberts, A., Jancarik, J., Yokota, H., Kim, R., Wemmer, D.E., and Kim, S.-H. (2003). Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima. Protein Sci. 12, 1464-1472.
    • (2003) Protein Sci. , vol.12 , pp. 1464-1472
    • Shin, D.H.1    Roberts, A.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Wemmer, D.E.6    Kim, S.-H.7
  • 30
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000). Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 31
    • 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
  • 32
    • 0024237631 scopus 로고
    • Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein
    • Vyas, N.K., Vyas, M.N., and 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
  • 33
    • 0035155638 scopus 로고    scopus 로고
    • Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 Å resolution
    • Wang, W., Kim, R., Jancarik, J., Yokota, H., and Kim, S.-H. (2001). Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 Å resolution. Structure 9, 65-71.
    • (2001) Structure , vol.9 , pp. 65-71
    • Wang, W.1    Kim, R.2    Jancarik, J.3    Yokota, H.4    Kim, S.-H.5
  • 34
    • 0031975752 scopus 로고    scopus 로고
    • Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
    • Welch, M., Chinardet, N., Mourey, L., Birck, C., and Samama, J.-P. (1998). Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nat. Struct. Biol. 5, 25-29.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 25-29
    • Welch, M.1    Chinardet, N.2    Mourey, L.3    Birck, C.4    Samama, J.-P.5
  • 35
    • 2142646427 scopus 로고    scopus 로고
    • Investigation of metal ion binding in phosphonoacetaldehyde hydrolase identifies sequence markers for metal-activated enzymes of the HAD enzyme superfamily
    • Zhang, G., Morais, M.C., Dai, J., Dunaway-Mariano, D., and Allen, K.N. (2004). Investigation of metal ion binding in phosphonoacetaldehyde hydrolase identifies sequence markers for metal-activated enzymes of the HAD enzyme superfamily. Biochemistry 43, 4990-4997.
    • (2004) Biochemistry , vol.43 , pp. 4990-4997
    • Zhang, G.1    Morais, M.C.2    Dai, J.3    Dunaway-Mariano, D.4    Allen, K.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.