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Volumn 385, Issue 2, 2009, Pages 653-664

Collective motions in Glucosamine-6-phosphate Synthase: Influence of Ligand Binding and role in Ammonia Channelling and Opening of the Fructose-6-Phosphate Binding Site

Author keywords

ammonia channelling; binding site opening; glucosamine 6 phosphate synthase; ligand binding; normal mode analysis

Indexed keywords

AMMONIA; BACTERIAL ENZYME; FRUCTOSE 6 PHOSPHATE; GLUTAMINE; GLUTAMINE FRUCTOSE 6 PHOSPHATE AMINOTRANSFERASE;

EID: 58149103168     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.10.032     Document Type: Article
Times cited : (38)

References (27)
  • 2
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 414 (2001) 813-820
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 3
    • 33644873810 scopus 로고    scopus 로고
    • Hexosamines, insulin resistance, and the complications of diabetes: current status
    • Buse M.G. Hexosamines, insulin resistance, and the complications of diabetes: current status. Am. J. Physiol. Endocrinol. Metab. 290 (2006) E1-E8
    • (2006) Am. J. Physiol. Endocrinol. Metab. , vol.290
    • Buse, M.G.1
  • 4
    • 0025851177 scopus 로고
    • Glucosamine-6-phosphate synthase from E. Coli Yields two proteins upon limited proteolysis: identification of the gluttamine aminohydrolase and 2R ketose/aldose isomerase-bearing domains based on their biochemical properties
    • Denisot M.A., Le Goffic F., and Badet B. Glucosamine-6-phosphate synthase from E. Coli Yields two proteins upon limited proteolysis: identification of the gluttamine aminohydrolase and 2R ketose/aldose isomerase-bearing domains based on their biochemical properties. Arch. Biochem. Biophys. 288 (1991) 225-230
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 225-230
    • Denisot, M.A.1    Le Goffic, F.2    Badet, B.3
  • 8
    • 40849146802 scopus 로고    scopus 로고
    • Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel
    • Mouilleron S., Badet-Denisot M.A., and Golinelli-Pimpaneau B. Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel. J. Mol. Biol. 377 (2008) 1174-1185
    • (2008) J. Mol. Biol. , vol.377 , pp. 1174-1185
    • Mouilleron, S.1    Badet-Denisot, M.A.2    Golinelli-Pimpaneau, B.3
  • 9
    • 34250194661 scopus 로고    scopus 로고
    • Ammonia channeling in bacterial glucosamine-6-phosphate synthase (Glms): Molecular dynamics simulations and kinetic studies of protein mutants
    • Floquet N., Mouilleron S., Daher R., Maigret B., Badet B., and Badet-Denisot M.A. Ammonia channeling in bacterial glucosamine-6-phosphate synthase (Glms): Molecular dynamics simulations and kinetic studies of protein mutants. FEBS Lett. 581 (2007) 2981-2987
    • (2007) FEBS Lett. , vol.581 , pp. 2981-2987
    • Floquet, N.1    Mouilleron, S.2    Daher, R.3    Maigret, B.4    Badet, B.5    Badet-Denisot, M.A.6
  • 10
    • 0034127361 scopus 로고    scopus 로고
    • Collective protein dynamics in relation to function
    • Berendsen H.J., and Hayward S. Collective protein dynamics in relation to function. Curr. Opin. Struct. Biol. 10 (2000) 165-169
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 165-169
    • Berendsen, H.J.1    Hayward, S.2
  • 11
    • 51249115387 scopus 로고    scopus 로고
    • Human thrombospondin's (TSP-1) C-terminal domain opens to interact with the CD-47 receptor: a molecular modeling study
    • Floquet N., Dedieu S., Martiny L., Dauchez M., and Perahia D. Human thrombospondin's (TSP-1) C-terminal domain opens to interact with the CD-47 receptor: a molecular modeling study. Arch. Biochem. Biophys. 478 (2008) 103-109
    • (2008) Arch. Biochem. Biophys. , vol.478 , pp. 103-109
    • Floquet, N.1    Dedieu, S.2    Martiny, L.3    Dauchez, M.4    Perahia, D.5
  • 12
    • 33748759844 scopus 로고    scopus 로고
    • Normal mode analysis as a prerequisite for drug design: application to matrix metalloproteinases inhibitors
    • Floquet N., Marechal J.D., Badet-Denisot M.A., Robert C.H., Dauchez M., and Perahia D. Normal mode analysis as a prerequisite for drug design: application to matrix metalloproteinases inhibitors. FEBS Lett. 580 (2006) 5130-5136
    • (2006) FEBS Lett. , vol.580 , pp. 5130-5136
    • Floquet, N.1    Marechal, J.D.2    Badet-Denisot, M.A.3    Robert, C.H.4    Dauchez, M.5    Perahia, D.6
  • 13
    • 33645240462 scopus 로고    scopus 로고
    • Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase
    • Mouilleron S., Badet-Denisot M.A., and Golinelli-Pimpaneau B. Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase. J. Biol. Chem. 281 (2006) 4404-4412
    • (2006) J. Biol. Chem. , vol.281 , pp. 4404-4412
    • Mouilleron, S.1    Badet-Denisot, M.A.2    Golinelli-Pimpaneau, B.3
  • 14
    • 50449105242 scopus 로고    scopus 로고
    • Use of normal modes for structural modelling of proteins: the case study of rat heme-oxygenase 1
    • Maréchal J.D., and Perahia D. Use of normal modes for structural modelling of proteins: the case study of rat heme-oxygenase 1. Eur. J. Biophys. 37 (2008) 1157-1165
    • (2008) Eur. J. Biophys. , vol.37 , pp. 1157-1165
    • Maréchal, J.D.1    Perahia, D.2
  • 15
    • 33847262173 scopus 로고    scopus 로고
    • Domain motions of glucosamine-6P synthase: comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation
    • Mouilleron S., and Golinelli-Pimpaneau B. Domain motions of glucosamine-6P synthase: comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation. Protein Sci. 16 (2007) 485-493
    • (2007) Protein Sci. , vol.16 , pp. 485-493
    • Mouilleron, S.1    Golinelli-Pimpaneau, B.2
  • 17
    • 0036007874 scopus 로고    scopus 로고
    • From Lobry de Bruyn to enzyme-catalyzed ammonia channelling: molecular studies of D-glucosamine-6P synthase
    • Teplyakov A., Leriche C., Obmolova G., Badet B., and Badet-Denisot M.A. From Lobry de Bruyn to enzyme-catalyzed ammonia channelling: molecular studies of D-glucosamine-6P synthase. Nature Prod. Rep. 19 (2002) 60-69
    • (2002) Nature Prod. Rep. , vol.19 , pp. 60-69
    • Teplyakov, A.1    Leriche, C.2    Obmolova, G.3    Badet, B.4    Badet-Denisot, M.A.5
  • 21
    • 0032529009 scopus 로고    scopus 로고
    • Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 Å crystal structure of the isomerase domain
    • Teplyakov A., Obmolova G., Badet-Denisot M.A., Badet B., and Polikarpov. Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 Å crystal structure of the isomerase domain. Structure 6 (1998) 1047-1055
    • (1998) Structure , vol.6 , pp. 1047-1055
    • Teplyakov, A.1    Obmolova, G.2    Badet-Denisot, M.A.3    Badet, B.4    Polikarpov5
  • 22
    • 0029374782 scopus 로고
    • Computation of low-frequency normal modes in macromolecules: improvements to the method of diagonalization in a mixed basis and application to hemoglobin
    • Perahia D., and Mouawad L. Computation of low-frequency normal modes in macromolecules: improvements to the method of diagonalization in a mixed basis and application to hemoglobin. Comput. Chem. 19 (1995) 241-246
    • (1995) Comput. Chem. , vol.19 , pp. 241-246
    • Perahia, D.1    Mouawad, L.2
  • 23
    • 0029633176 scopus 로고
    • A method to explore transition in macromolecules. Applications to hemoglobin and phosphoglycerate kinase
    • Guilbert C., Perahia D., and Mouawad L. A method to explore transition in macromolecules. Applications to hemoglobin and phosphoglycerate kinase. Comput. Phys. Commun. 91 (1995) 263-273
    • (1995) Comput. Phys. Commun. , vol.91 , pp. 263-273
    • Guilbert, C.1    Perahia, D.2    Mouawad, L.3
  • 24
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme
    • Hayward S., and Berendsen H.J. Systematic analysis of domain motions in proteins from conformational change: new results on citrate synthase and T4 lysozyme. Proteins: Struct. Funct. Genet. 30 (1998) 144-154
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 25
    • 0030888546 scopus 로고    scopus 로고
    • Model-free methods of analyzing domain motions in proteins from simulation: a comparison of normal mode analysis and molecular dynamics simulation of lysozyme
    • Hayward S., Kitao A., and Berendsen H.J. Model-free methods of analyzing domain motions in proteins from simulation: a comparison of normal mode analysis and molecular dynamics simulation of lysozyme. Proteins: Struct. Funct. Genet. 27 (1997) 425-437
    • (1997) Proteins: Struct. Funct. Genet. , vol.27 , pp. 425-437
    • Hayward, S.1    Kitao, A.2    Berendsen, H.J.3
  • 26
    • 0014054519 scopus 로고
    • The detection of disease clustering and a generalized regression approach
    • Mantel N. The detection of disease clustering and a generalized regression approach. Cancer Res. 27 (1967) 209-220
    • (1967) Cancer Res. , vol.27 , pp. 209-220
    • Mantel, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.