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Volumn 372, Issue 3, 2007, Pages 672-688

The Crystal and Solution Studies of Glucosamine-6-phosphate Synthase from Candida albicans

Author keywords

aldose ketose isomerase; crystal structure; glucosamine 6 phosphate synthase; solution structure

Indexed keywords

2 AMINO 2 DEOXY DEXTRO MANNITOL 6 PHOSPHATE; FRUCTOSE 6 PHOSPHATE; GLUCOSAMINE DERIVATIVE; GLUCOSE 6 PHOSPHATE; GLUTAMINE FRUCTOSE 6 PHOSPHATE AMINOTRANSFERASE; PHOSPHATE; UNCLASSIFIED DRUG; URIDINE 5' DIPHOSPHO N ACETYL D GLUCOSAMINE;

EID: 34548277126     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.07.002     Document Type: Article
Times cited : (33)

References (42)
  • 1
    • 9544226451 scopus 로고    scopus 로고
    • Overexpression of glutamine:fructose-6-phosphate amidotransferase in transgenic mice leads to insulin resistance
    • Hebert L.F., Daniels M.C., Zhou J., Crook E.D., Turner R.L., Simmons S.T., et al. Overexpression of glutamine:fructose-6-phosphate amidotransferase in transgenic mice leads to insulin resistance. J. Clin. Invest. 98 (1996) 930-936
    • (1996) J. Clin. Invest. , vol.98 , pp. 930-936
    • Hebert, L.F.1    Daniels, M.C.2    Zhou, J.3    Crook, E.D.4    Turner, R.L.5    Simmons, S.T.6
  • 2
    • 0028226560 scopus 로고
    • Mucosal glucosamine synthetase activity on inflammatory bowel disease
    • Winslet M.C., Poxon V., Allan A., and Keighley M.R. Mucosal glucosamine synthetase activity on inflammatory bowel disease. Dig. Dis. Sci. 39 (1994) 540-544
    • (1994) Dig. Dis. Sci. , vol.39 , pp. 540-544
    • Winslet, M.C.1    Poxon, V.2    Allan, A.3    Keighley, M.R.4
  • 3
    • 0033914401 scopus 로고    scopus 로고
    • Novel approaches in the rational design of antifungal agents of low toxicity
    • Borowski E. Novel approaches in the rational design of antifungal agents of low toxicity. Farmaco 55 (2000) 206-208
    • (2000) Farmaco , vol.55 , pp. 206-208
    • Borowski, E.1
  • 5
    • 0030586024 scopus 로고    scopus 로고
    • Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 Å structure of the glutaminase domain of glucosamine-6-phosphate synthase
    • Isupov M.N., Obmolova G., Butterworth S., Badet-Denisot M.-A., Badet B., Polikarpov I., et al. Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 Å structure of the glutaminase domain of glucosamine-6-phosphate synthase. Structure 4 (1996) 801-810
    • (1996) Structure , vol.4 , pp. 801-810
    • Isupov, M.N.1    Obmolova, G.2    Butterworth, S.3    Badet-Denisot, M.-A.4    Badet, B.5    Polikarpov, I.6
  • 6
    • 0032529009 scopus 로고    scopus 로고
    • Involvement of the C-terminus in intramolecular channeling in glucosamine-6-phosphate synthase: evidence from a 1.6 Å structure of the isomerase domain
    • Teplyakov A., Obmolova G., Badet-Denisot M.-A., Badet B., and Polikarpov I. Involvement of the C-terminus in intramolecular channeling in glucosamine-6-phosphate synthase: evidence from a 1.6 Å 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    Polikarpov, I.5
  • 7
    • 0033019834 scopus 로고    scopus 로고
    • The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase
    • Teplyakov A., Obmolova G., Badet-Denisot M.-A., and Badet B. The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase. Protein Sci. 8 (1999) 596-602
    • (1999) Protein Sci. , vol.8 , pp. 596-602
    • Teplyakov, A.1    Obmolova, G.2    Badet-Denisot, M.-A.3    Badet, B.4
  • 8
    • 0036007874 scopus 로고    scopus 로고
    • From Lobry de Bruyn to enzyme-catalyzed ammonia channelling: molecular studies on 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 on 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
  • 9
    • 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
  • 10
  • 11
    • 0037013983 scopus 로고    scopus 로고
    • Glucosamine-6-phosphate synthase - the multifacets enzyme
    • Milewski S. Glucosamine-6-phosphate synthase - the multifacets enzyme. Biochim. Biophys. Acta 1597 (2002) 173-192
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 173-192
    • Milewski, S.1
  • 12
    • 11144275172 scopus 로고    scopus 로고
    • Molecular therapeutic target for type-2 diabetes
    • Chou K.-C. Molecular therapeutic target for type-2 diabetes. J. Proteome Res. 3 (2004) 1284-1288
    • (2004) J. Proteome Res. , vol.3 , pp. 1284-1288
    • Chou, K.-C.1
  • 13
    • 33744473334 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the isomerase domain of glucosamine-6-phosphate synthase from Candida albicans
    • Olchowy J., Je{ogonek}drzejczak R., Milewski S., and Rypniewski W. Crystallization and preliminary X-ray analysis of the isomerase domain of glucosamine-6-phosphate synthase from Candida albicans. Acta Crystallog. sect. F 61 (2005) 994-996
    • (2005) Acta Crystallog. sect. F , vol.61 , pp. 994-996
    • Olchowy, J.1    Jedrzejczak, R.2    Milewski, S.3    Rypniewski, W.4
  • 14
    • 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. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 15
    • 0242571958 scopus 로고    scopus 로고
    • Small angle scattering studies of biological macromolecules in solution
    • Svergun D.I., and Koch M.H.J. Small angle scattering studies of biological macromolecules in solution. Rep. Progr. Phys. 66 (2003) 1735-1782
    • (2003) Rep. Progr. Phys. , vol.66 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.J.2
  • 17
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 18
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89 (2005) 1237-1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 19
    • 0016628845 scopus 로고
    • Sporulation in D-glucosamine auxotrophs of Saccharomyces cerevisiae: meiosis with defective ascospore wall formation
    • Whelan W.L., and Ballou C.E. Sporulation in D-glucosamine auxotrophs of Saccharomyces cerevisiae: meiosis with defective ascospore wall formation. J. Bacteriol. 124 (1975) 1545-1557
    • (1975) J. Bacteriol. , vol.124 , pp. 1545-1557
    • Whelan, W.L.1    Ballou, C.E.2
  • 20
    • 0015010536 scopus 로고
    • Mutant of Escherichia coli K-12 defective in D-glucosamine biosynthesis
    • Sarvas M. Mutant of Escherichia coli K-12 defective in D-glucosamine biosynthesis. J. Bacteriol. 105 (1971) 467-471
    • (1971) J. Bacteriol. , vol.105 , pp. 467-471
    • Sarvas, M.1
  • 21
    • 0029742775 scopus 로고    scopus 로고
    • Hexosamines and insulin resistance
    • McClain D.A., and Crook E.D. Hexosamines and insulin resistance. Diabetes 45 (1996) 1003-1009
    • (1996) Diabetes , vol.45 , pp. 1003-1009
    • McClain, D.A.1    Crook, E.D.2
  • 22
    • 34249073191 scopus 로고    scopus 로고
    • Functional domains and interdomain communication in Candida albicans glucosamine-6-phosphate synthase
    • Olchowy J., Gabriel I., and Milewski S. Functional domains and interdomain communication in Candida albicans glucosamine-6-phosphate synthase. Biochem. J. 404 (2007) 121-130
    • (2007) Biochem. J. , vol.404 , pp. 121-130
    • Olchowy, J.1    Gabriel, I.2    Milewski, S.3
  • 23
    • 33646882795 scopus 로고    scopus 로고
    • Structural analogues of reactive intermediates as inhibitors of glucosamine-6-phosphate synthase and phosphoglucose isomerase
    • Milewski S., Janiak A., and Wojciechowski M. Structural analogues of reactive intermediates as inhibitors of glucosamine-6-phosphate synthase and phosphoglucose isomerase. Arch. Biochem. Biophys. 450 (2006) 39-49
    • (2006) Arch. Biochem. Biophys. , vol.450 , pp. 39-49
    • Milewski, S.1    Janiak, A.2    Wojciechowski, M.3
  • 24
    • 0032518669 scopus 로고    scopus 로고
    • Stereoselective synthesis of 5-methylphosphono-D-arabino hydroximolactone, inhibitor of glucosamine-6-phosphate synthase and phosphoglucose isomerase
    • Le Camus C., Chassagne A., Badet-Denisot M.-A., and Badet B. Stereoselective synthesis of 5-methylphosphono-D-arabino hydroximolactone, inhibitor of glucosamine-6-phosphate synthase and phosphoglucose isomerase. Tetrahedron Letters 39 (1998) 287-288
    • (1998) Tetrahedron Letters , vol.39 , pp. 287-288
    • Le Camus, C.1    Chassagne, A.2    Badet-Denisot, M.-A.3    Badet, B.4
  • 25
    • 0033848837 scopus 로고    scopus 로고
    • Purification to homogeneity of Candida albicans glucosamine-6-phosphate synthase overexpressed in Escherichia coli
    • Sachadyn P., Je{ogonek}drzejczak R., Milewski S., Kur J., and Borowski E. Purification to homogeneity of Candida albicans glucosamine-6-phosphate synthase overexpressed in Escherichia coli. Protein Expr. Purif. 19 (2000) 343-349
    • (2000) Protein Expr. Purif. , vol.19 , pp. 343-349
    • Sachadyn, P.1    Jedrzejczak, R.2    Milewski, S.3    Kur, J.4    Borowski, E.5
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. sect. D 53 (1997) 240-255
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 30
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams P.D., Pannu N.S., Read R.J., and Brunger A.T. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl Acad. Sci. USA 94 (1997) 5018-5023
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brunger, A.T.4
  • 31
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 32
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 33
    • 0024033744 scopus 로고
    • Data acquisition systems for linear and area X-ray detectors using delay line readout
    • Boulin C.J., Kempf R., Gabriel A., and Koch M.H.J. Data acquisition systems for linear and area X-ray detectors using delay line readout. Nucl. Instrum. Methods ser. A 269 (1988) 312-320
    • (1988) Nucl. Instrum. Methods ser. A , vol.269 , pp. 312-320
    • Boulin, C.J.1    Kempf, R.2    Gabriel, A.3    Koch, M.H.J.4
  • 35
    • 0027578071 scopus 로고
    • A direct indirect method of small-angle scattering data treatment
    • Svergun D.I. A direct indirect method of small-angle scattering data treatment. J. Appl. Crystallog. 26 (1993) 258-267
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 258-267
    • Svergun, D.I.1
  • 36
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux petits angles; application a l'etude de phenomenes ultramicroscopiques
    • Guinier A. La diffraction des rayons X aux petits angles; application a l'etude de phenomenes ultramicroscopiques. Ann. Phys. (Paris) 12 (1939) 161-231
    • (1939) Ann. Phys. (Paris) , vol.12 , pp. 161-231
    • Guinier, A.1
  • 37
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect transform methods using perceptual criteria. J. Appl. Crystallog. 25 (1992) 495-503
    • (1992) J. Appl. Crystallog. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 38
    • 0002720864 scopus 로고
    • General theory
    • Glatter O., and Kratky O. (Eds), Academic Press, London
    • Porod G. General theory. In: Glatter O., and Kratky O. (Eds). Small-Angle Scattering (1982), Academic Press, London 17-51
    • (1982) Small-Angle Scattering , pp. 17-51
    • Porod, G.1
  • 39
    • 0029185933 scopus 로고
    • CRYSOL: a program to evaluate X-ray solution scattering of biological macro-molecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL: a program to evaluate X-ray solution scattering of biological macro-molecules from atomic coordinates. J. Appl. Crystallog. 28 (1995) 768-773
    • (1995) J. Appl. Crystallog. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 40
    • 0036930752 scopus 로고    scopus 로고
    • Addition of missing loops and domains to protein models by X-ray solution scattering
    • Petoukhov M.V., Eady N.A., Brown K.A., and Svergun D.I. Addition of missing loops and domains to protein models by X-ray solution scattering. Biophys. J. 83 (2002) 3113-3125
    • (2002) Biophys. J. , vol.83 , pp. 3113-3125
    • Petoukhov, M.V.1    Eady, N.A.2    Brown, K.A.3    Svergun, D.I.4
  • 41
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun D.I., Petoukhov M.V., and Koch M.H.J. Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80 (2001) 2946-2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3


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