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Volumn 12, Issue 7, 2005, Pages 608-614

Structural dissection and high-throughput screening of mannosylglycerate synthase

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOCONJUGATE; GLYCOSYLTRANSFERASE; MANNOSE; MANNOSIDE; MANNOSYLGLYCERATE SYNTHASE; POLYSACCHARIDE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 22144432266     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb950     Document Type: Article
Times cited : (66)

References (28)
  • 1
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho, P., Deleury, E., Davies, G.J. & Henrissat, B. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328, 307-317 (2003).
    • (2003) J. Mol. Biol. , vol.328 , pp. 307-317
    • Coutinho, P.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 2
    • 0742288006 scopus 로고    scopus 로고
    • Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog
    • Chiu, C.P. et al. Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog. Nat. Struct. Mol. Biol. 11, 163-170 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 163-170
    • Chiu, C.P.1
  • 3
    • 0033580656 scopus 로고    scopus 로고
    • Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms
    • Charnock, S.J. & Davies, G.J. Structure of the nucleotide-diphospho- sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms. Biochemistry 38, 6380-6385 (1999).
    • (1999) Biochemistry , vol.38 , pp. 6380-6385
    • Charnock, S.J.1    Davies, G.J.2
  • 4
    • 0027965664 scopus 로고
    • Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose
    • Vrielink, A., Rüger, W., Driessen, H.P.C. & Freemont, P.S. Crystal structure of the DNA modifying enzyme β-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBOJ. 13, 3413-3422 (1994).
    • (1994) EMBOJ. , vol.13 , pp. 3413-3422
    • Vrielink, A.1    Rüger, W.2    Driessen, H.P.C.3    Freemont, P.S.4
  • 5
    • 2342420346 scopus 로고    scopus 로고
    • Structure of Kre2p/Mnt1p-a yeast α-1,2-mannosyltransferase involved in mannoprotein biosynthesis
    • Lobsanov, Y.D. et al. Structure of Kre2p/Mnt1p-a yeast α-1,2-mannosyltransferase involved in mannoprotein biosynthesis. J. Biol. Chem. 279, 17921-17931 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 17921-17931
    • Lobsanov, Y.D.1
  • 6
    • 0033544948 scopus 로고    scopus 로고
    • Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus-Biochemical and genetic characterization of a mannosylglycerate synthase
    • Martins, L.O. et al. Biosynthesis of mannosylglycerate in the thermophilic bacterium Rhodothermus marinus-Biochemical and genetic characterization of a mannosylglycerate synthase. J. Biol. Chem. 274, 35407-35414 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 35407-35414
    • Martins, L.O.1
  • 7
    • 1642279326 scopus 로고    scopus 로고
    • Specialized roles of the two pathways for the synthesis of mannosylglycerate in osmoadaptation and thermoadaptation of Rhodothermus marinus
    • Borges, N., Marugg, J.D., Empadinhas, N., da Costa, M.S. & Santos, H. Specialized roles of the two pathways for the synthesis of mannosylglycerate in osmoadaptation and thermoadaptation of Rhodothermus marinus. J. Biol. Chem. 279, 9892-9898 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 9892-9898
    • Borges, N.1    Marugg, J.D.2    Empadinhas, N.3    Da Costa, M.S.4    Santos, H.5
  • 8
    • 0036599177 scopus 로고    scopus 로고
    • Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes
    • Borges, N., Ramos, A., Raven, N.D.H., Sharp, R.J. & Santos, H. Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes. Extremophiles 6, 209-216 (2002).
    • (2002) Extremophiles , vol.6 , pp. 209-216
    • Borges, N.1    Ramos, A.2    Raven, N.D.H.3    Sharp, R.J.4    Santos, H.5
  • 9
    • 0042970474 scopus 로고    scopus 로고
    • Protein stabilisation by compatible solutes: Effect of mannosylglycerate on unfolding thermodynamics and activity of ribonuclease A
    • Faria, T.Q., Knapp, S., Ladenstein, R., Macanita, A.L. & Santos, H. Protein stabilisation by compatible solutes: Effect of mannosylglycerate on unfolding thermodynamics and activity of ribonuclease A. Chembiochem 4, 734-741 (2003).
    • (2003) Chembiochem , vol.4 , pp. 734-741
    • Faria, T.Q.1    Knapp, S.2    Ladenstein, R.3    Macanita, A.L.4    Santos, H.5
  • 10
    • 21144450850 scopus 로고    scopus 로고
    • High-throughput mass spectrometry monitoring for multi-substrate enzymes: Determining the kinetic parameters and catalytic activities of glycosyltransferases
    • Yang, M., Brazier, M., Edwards, R. & Davis, B.H. High-throughput mass spectrometry monitoring for multi-substrate enzymes: determining the kinetic parameters and catalytic activities of glycosyltransferases. Chembiochem 6, 346-357 (2005).
    • (2005) Chembiochem , vol.6 , pp. 346-357
    • Yang, M.1    Brazier, M.2    Edwards, R.3    Davis, B.H.4
  • 11
    • 0037229829 scopus 로고    scopus 로고
    • Synthesis of GDP-mannose and mannosylglycerate from labeled mannose by genetically engineered Escherichia coll without loss of specific isotopic enrichment
    • Sampaio, M.M., Santos, H. & Boos, W. Synthesis of GDP-mannose and mannosylglycerate from labeled mannose by genetically engineered Escherichia coll without loss of specific isotopic enrichment. Appl. Environ. Microbiol. 69, 233-240 (2003).
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 233-240
    • Sampaio, M.M.1    Santos, H.2    Boos, W.3
  • 12
    • 0032493440 scopus 로고    scopus 로고
    • Activity of the yeast MNN1 α-1,3-mannosyltransferase requires a motif conserved in many other glycosyltransferase families
    • Wiggins, C.A. & Munro, S. Activity of the yeast MNN1 α-1,3-mannosyltransferase requires a motif conserved in many other glycosyltransferase families. Proc. Natl. Acad. Sci. USA 95, 7945-7950 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7945-7950
    • Wiggins, C.A.1    Munro, S.2
  • 13
    • 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. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 14
    • 0012784535 scopus 로고    scopus 로고
    • Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis
    • Pedersen, L.C. et al. Crystal structure of an alpha 1,4-N- acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. J. Biol. Chem. 278, 14420-14428 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14420-14428
    • Pedersen, L.C.1
  • 15
    • 0035151023 scopus 로고    scopus 로고
    • Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs
    • Persson, K. et al. Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs. Nat. Struct. Biol. 8, 166-175 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 166-175
    • Persson, K.1
  • 16
    • 0030843984 scopus 로고    scopus 로고
    • A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino-acid similarities
    • Campbell, J.A., Davies, G.J., Bulone, V. & Henrissat, B. A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino-acid similarities. Biochem. J. 326, 929-942 (1997).
    • (1997) Biochem. J. , vol.326 , pp. 929-942
    • Campbell, J.A.1    Davies, G.J.2    Bulone, V.3    Henrissat, B.4
  • 17
    • 3142615417 scopus 로고    scopus 로고
    • Intermediate trapping on a mutant retaining α-galactosyltransferase identifies an unexpected aspartate residue
    • Lairson, L.L. et al. Intermediate trapping on a mutant retaining α-galactosyltransferase identifies an unexpected aspartate residue. J. Biol. Chem. 279, 28339-28344 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 28339-28344
    • Lairson, L.L.1
  • 18
    • 0001403866 scopus 로고
    • Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2,2,2-trifluoroethano
    • Sinnott, M.L. & Jencks, W. Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2,2,2-trifluoroethano. J. Am. Chem. Soc. 102, 2026-2032 (1980).
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2026-2032
    • Sinnott, M.L.1    Jencks, W.2
  • 19
    • 14544271931 scopus 로고    scopus 로고
    • Tailored catalysts for plant cell-wall degradation: Redesigning the exo/endo preference of the Cellvibrio japonicus arabinanase 43A
    • Proctor, M. et al. Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of the Cellvibrio japonicus arabinanase 43A. Proc. Natl. Acad. Sci. USA 102, 2697-2702 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2697-2702
    • Proctor, M.1
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
  • 23
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger, AT. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 24
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (1997).
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 25
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum likelihood method
    • Murshudov, G.N., Vagin, A.A. & Dodson, E.J. Refinement of macromolecular structures by the maximum likelihood method. Acts Crystallogr. 053, 240-255 (1997).
    • (1997) Acts Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 26
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 132-134 (1997).
    • (1997) J. Mol. Graph. Model. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 27
    • 0034602394 scopus 로고    scopus 로고
    • Heparan/chondroitin sulfate biosynthesis: Structure and mechanism of human glucuronyltransferase I
    • Pedersen, L.C. et al. Heparan/chondroitin sulfate biosynthesis: structure and mechanism of human glucuronyltransferase I. J. Biol. Chem. 275, 34580-34-585 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 34580-34585
    • Pedersen, L.C.1
  • 28
    • 0035824876 scopus 로고    scopus 로고
    • Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: A comparison with related NDP-sugar glycosyltransferases
    • Tarbouriech, N., Charnock, S.J. & Davies, G.J. Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases. J. Mol. Biol. 314, 655-661 (2001).
    • (2001) J. Mol. Biol. , vol.314 , pp. 655-661
    • Tarbouriech, N.1    Charnock, S.J.2    Davies, G.J.3


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