메뉴 건너뛰기




Volumn 282, Issue 3, 1998, Pages 667-681

A 2.8 Å resolution structure of B-phosphogluconate dehydrogenase from the protozoan parasite Trypanosoma brucei: Comparison with the sheep enzyme accounts for differences in activity with coenzyme and substrate analogues

Author keywords

6 phosphogluconate; Dehydrogenase; NADP; T. brucei; X ray structure

Indexed keywords

DIMER; LIVER ENZYME; MONOMER; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHOSPHOGLUCONATE DEHYDROGENASE; PROTOZOAL PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0032566440     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2059     Document Type: Article
Times cited : (54)

References (42)
  • 1
    • 0018499005 scopus 로고
    • Binding of coenzyme and substrate and coenzyme analogues to 6-phosphogluconate dehydrogenase from sheep liver
    • Abdallah, M. A., Adams, M. J., Archibald, I. G., Biellmann, J.-F., Helliwell, J. R. & Jenkins, S. E. (1979). Binding of coenzyme and substrate and coenzyme analogues to 6-phosphogluconate dehydrogenase from sheep liver. Eur. J. Biochem. 98, 121-130.
    • (1979) Eur. J. Biochem. , vol.98 , pp. 121-130
    • Abdallah, M.A.1    Adams, M.J.2    Archibald, I.G.3    Biellmann, J.-F.4    Helliwell, J.R.5    Jenkins, S.E.6
  • 2
    • 0028773899 scopus 로고
    • Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: Implications for NADP specificity and the enzyme mechanism
    • Adams, M. J., Ellis, G. H., Gover, S., Naylor, C. E. & Phillips, C. (1994). Crystallographic study of coenzyme, coenzyme analogue and substrate binding in 6-phosphogluconate dehydrogenase: implications for NADP specificity and the enzyme mechanism. Structure, 2, 651-668.
    • (1994) Structure , vol.2 , pp. 651-668
    • Adams, M.J.1    Ellis, G.H.2    Gover, S.3    Naylor, C.E.4    Phillips, C.5
  • 3
    • 0031032145 scopus 로고    scopus 로고
    • The pentose phosphate pathway and parasitic protozoa
    • Barrett, M. P. (1997). The pentose phosphate pathway and parasitic protozoa. Parasitol. Today, 13, 11-16.
    • (1997) Parasitol. Today , vol.13 , pp. 11-16
    • Barrett, M.P.1
  • 4
    • 0027404204 scopus 로고
    • A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei
    • Barrett, M. P. & Le, Page R. W. F. (1993). A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei. Mol. Biochem. Parasitol. 57, 89-100.
    • (1993) Mol. Biochem. Parasitol. , vol.57 , pp. 89-100
    • Barrett, M.P.1    Le Page, R.W.F.2
  • 5
    • 0028370475 scopus 로고
    • Overexpression in Escherichia coli and purification of the 6-phosphogluconate dehydrogenase of Trypanosoma brucei
    • Barrett, M. P., Phillips, C., Adams, M. J. & Le, Page R. W. F. (1994). Overexpression in Escherichia coli and purification of the 6-phosphogluconate dehydrogenase of Trypanosoma brucei. Protein Expr. Purif. 5, 44-49.
    • (1994) Protein Expr. Purif. , vol.5 , pp. 44-49
    • Barrett, M.P.1    Phillips, C.2    Adams, M.J.3    Le Page, R.W.F.4
  • 6
    • 0025303764 scopus 로고
    • Protein multiple sequence alignment and flexible pattern matching
    • Barton, G. J. (1990). Protein multiple sequence alignment and flexible pattern matching. Methods Enzymol. 183, 403-428.
    • (1990) Methods Enzymol. , vol.183 , pp. 403-428
    • Barton, G.J.1
  • 7
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation
    • Bernstein, B. E., Michels, P. A. M. & Hol, W. G. J. (1997). Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. Nature, 385, 275-278.
    • (1997) Nature , vol.385 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.M.2    Hol, W.G.J.3
  • 9
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992b). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 10
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 11
    • 0024497978 scopus 로고
    • The enzymes of the classical pentose phosphate pathway display differential activities in the procyclic and bloodstream forms of Trypanosoma brucei
    • Cronin, C. N., Nolan, D. P. & Voorheis, H. P. (1989). The enzymes of the classical pentose phosphate pathway display differential activities in the procyclic and bloodstream forms of Trypanosoma brucei. FEBS Letters, 244, 26-30.
    • (1989) FEBS Letters , vol.244 , pp. 26-30
    • Cronin, C.N.1    Nolan, D.P.2    Voorheis, H.P.3
  • 12
    • 0015581903 scopus 로고
    • Sheep liver 6-phosphogluconate dehydrogenase: Isolation procedure and effect of pH, ionic strength and metal ions on the kinetic parameters
    • Dyson, J. E. D., D'Orazio, R. E. & Hanson, W. H. (1973). Sheep liver 6-phosphogluconate dehydrogenase: isolation procedure and effect of pH, ionic strength and metal ions on the kinetic parameters. Arch. Biochem. Biophys. 154, 623-635.
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 623-635
    • Dyson, J.E.D.1    D'Orazio, R.E.2    Hanson, W.H.3
  • 13
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A, 47, 392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 14
    • 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. 15, 132-134.
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 15
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the kinetoplastida
    • Fairlamb, A. H. & Cerami, A. (1992). Metabolism and functions of trypanothione in the kinetoplastida. Annu. Rev. Microbiol. 46, 695-729.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 16
    • 0022040857 scopus 로고
    • Introduction to trypanosomiasis
    • Goodwin, L. G. (1985). Introduction to trypanosomiasis. Brit. Med. Bull. 42, 103-104.
    • (1985) Brit. Med. Bull. , vol.42 , pp. 103-104
    • Goodwin, L.G.1
  • 17
    • 0026779219 scopus 로고
    • Subunit asymmetry in the ternary complex of lamb liver 6-phosphogluconate dehydrogenase detected by a NADP analogue
    • Hanau, S., Dallocchio, F. & Rippa, M. (1992). Subunit asymmetry in the ternary complex of lamb liver 6-phosphogluconate dehydrogenase detected by a NADP analogue. Biochim. Biophys. Acta, 1159, 262-266.
    • (1992) Biochim. Biophys. Acta , vol.1159 , pp. 262-266
    • Hanau, S.1    Dallocchio, F.2    Rippa, M.3
  • 18
    • 0029742699 scopus 로고    scopus 로고
    • 6-Phosphogluconate dehydrogenase from Trypanosoma brucei. Kinetic analysis and inhibition by trypanocidal drugs
    • Hanau, S., Rippa, M., Bertelli, M., Dallocchio, F. & Barrett, M. P. (1996). 6-Phosphogluconate dehydrogenase from Trypanosoma brucei. Kinetic analysis and inhibition by trypanocidal drugs. Eur. J. Biochem. 240, 592-599.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 592-599
    • Hanau, S.1    Rippa, M.2    Bertelli, M.3    Dallocchio, F.4    Barrett, M.P.5
  • 19
    • 0028339865 scopus 로고
    • Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli 09:K30 and participation of rfb genes in the synthesis of the group 1 K30 capsular polysaccharide
    • Jayaratne, P., Bronner, D., Maclachlan, R. P., Dodgson, C., Kido, N. & Whitfield, C. (1994). Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli 09:K30 and participation of rfb genes in the synthesis of the group 1 K30 capsular polysaccharide. J. Bacteriol. 176, 3126-3139.
    • (1994) J. Bacteriol. , vol.176 , pp. 3126-3139
    • Jayaratne, P.1    Bronner, D.2    Maclachlan, R.P.3    Dodgson, C.4    Kido, N.5    Whitfield, C.6
  • 20
    • 0022333120 scopus 로고
    • Interactive computer graphics: FRODO
    • Jones, T. A. (1985). Interactive computer graphics: FRODO. Methods Enzymol. 115, 157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 21
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thorton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thorton, J.M.4
  • 24
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • SERC, Daresbury Laboratory, Warrington, UK
    • Leslie, A. G. W. (1992). Recent changes to the MOSFLM package for processing film and image plate data. In Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography, p. 26, SERC, Daresbury Laboratory, Warrington, UK.
    • (1992) Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography , pp. 26
    • Leslie, A.G.W.1
  • 25
    • 0001585429 scopus 로고
    • Glucose 6-phosphate dehydrogenase deficiency
    • (Scriver, C. L., Beaudet, A. L., Sly, W. S. & Valle, D., eds), 7th edit., McGraw-Hill, New York
    • Luzzatto, L. & Mehta, A. (1995). Glucose 6-phosphate dehydrogenase deficiency. In The Metabolic and Molecular Basis Of Inherited Disease (Scriver, C. L., Beaudet, A. L., Sly, W. S. & Valle, D., eds), vol. III, 7th edit., pp. 3367-3398, McGraw-Hill, New York.
    • (1995) The Metabolic and Molecular Basis of Inherited Disease , vol.3 , pp. 3367-3398
    • Luzzatto, L.1    Mehta, A.2
  • 26
    • 0028298146 scopus 로고
    • Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme
    • Mande, S. C., Mainfroid, V., Kalk, K. H., Goraj, K., Martial, J. A. & Hol, W. G. J. (1994). Crystal structure of recombinant human triosephosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci. 3, 810-821.
    • (1994) Protein Sci. , vol.3 , pp. 810-821
    • Mande, S.C.1    Mainfroid, V.2    Kalk, K.H.3    Goraj, K.4    Martial, J.A.5    Hol, W.G.J.6
  • 27
    • 0028834278 scopus 로고
    • Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress
    • Pandolfi, P. P., Sonati, F., Rivi, R., Mason, P., Grosveld, F. & Luzzatto, L. (1995). Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J. 14, 5209-5215.
    • (1995) EMBO J. , vol.14 , pp. 5209-5215
    • Pandolfi, P.P.1    Sonati, F.2    Rivi, R.3    Mason, P.4    Grosveld, F.5    Luzzatto, L.6
  • 28
    • 0027491529 scopus 로고
    • Preliminary crystallographic study of 6-phosphogluconate dehydrogenase from Trypanosoma brucei
    • Phillips, C., Barrett, M. P., Gover, S., Le, Page R. W. F. & Adams, M. J. (1993). Preliminary crystallographic study of 6-phosphogluconate dehydrogenase from Trypanosoma brucei. J. Mol. Biol. 233, 317-321.
    • (1993) J. Mol. Biol. , vol.233 , pp. 317-321
    • Phillips, C.1    Barrett, M.P.2    Gover, S.3    Le Page, R.W.F.4    Adams, M.J.5
  • 29
    • 0029108068 scopus 로고
    • Structure of 6-phosphogluconate dehydrogenase refined at 2 A resolution
    • Phillips, C., Gover, S. & Adams, M. J. (1995). Structure of 6-phosphogluconate dehydrogenase refined at 2 A resolution. Acta Crystallog. sect. D, 51, 290-304.
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 290-304
    • Phillips, C.1    Gover, S.2    Adams, M.J.3
  • 30
    • 0030589731 scopus 로고    scopus 로고
    • Kinetic and chemical mechanism of the sheep liver 6-phosphogluconate dehydrogenase
    • Price, N. E. & Cook, P. F. (1996). Kinetic and chemical mechanism of the sheep liver 6-phosphogluconate dehydrogenase. Arch. Biochem. Biophys. 336, 215-223.
    • (1996) Arch. Biochem. Biophys. , vol.336 , pp. 215-223
    • Price, N.E.1    Cook, P.F.2
  • 31
    • 0023318540 scopus 로고
    • The biochemistry of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase
    • Rosemeyer, M. A. (1987). The biochemistry of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase. Cell Biochem. Funct. 5, 79-95.
    • (1987) Cell Biochem. Funct. , vol.5 , pp. 79-95
    • Rosemeyer, M.A.1
  • 32
    • 0031566432 scopus 로고    scopus 로고
    • Recognition of analogous and homologous protein folds: Analysis of sequence and structure conservation
    • Russell, R. B., Saqi, M. A. S., Sayle, R. A., Bates, P. A. & Sternberg, M. J. E. (1997). Recognition of analogous and homologous protein folds: analysis of sequence and structure conservation. J. Mol. Biol. 269, 423-429.
    • (1997) J. Mol. Biol. , vol.269 , pp. 423-429
    • Russell, R.B.1    Saqi, M.A.S.2    Sayle, R.A.3    Bates, P.A.4    Sternberg, M.J.E.5
  • 33
    • 0027064669 scopus 로고
    • Sequence of sheep 6-phosphogluconate dehydrogenase
    • Somers, D. O'N., Medd, S., Walker, J. E. & Adams, M. J. (1992). Sequence of sheep 6-phosphogluconate dehydrogenase. Biochem. J. 288, 1061-1067.
    • (1992) Biochem. J. , vol.288 , pp. 1061-1067
    • O'N, S.D.1    Medd, S.2    Walker, J.E.3    Adams, M.J.4
  • 34
    • 0023040151 scopus 로고
    • Kinetic studies of 6-phosphogluconate dehydrogenase from sheep liver
    • Topham, C. M., Matthews, B. & Dalziel, K. (1986). Kinetic studies of 6-phosphogluconate dehydrogenase from sheep liver. Eur. J. Biochem. 156, 555-567.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 555-567
    • Topham, C.M.1    Matthews, B.2    Dalziel, K.3
  • 35
    • 0030454628 scopus 로고    scopus 로고
    • Identification of a cDNA encoding 6-phosphogluconate dehydrogenase from a human heart cDNA library
    • Tsui, S. K., Chan, J. Y., Waye, M. M., Fung, K. P. & Lee, C. Y. (1996). Identification of a cDNA encoding 6-phosphogluconate dehydrogenase from a human heart cDNA library. Biochem. Genet. 34, 367-373.
    • (1996) Biochem. Genet. , vol.34 , pp. 367-373
    • Tsui, S.K.1    Chan, J.Y.2    Waye, M.M.3    Fung, K.P.4    Lee, C.Y.5
  • 36
    • 0028090162 scopus 로고
    • Selective inhibition of trypanosomal glyceraldehyde-3-phosphate dehydrogenase by protein structure-based design: Toward new drugs for the treatment of sleeping sickness
    • Verlinde, C. L. M. J., Callens, M., Van Calenbergh, S., Van Aerschot, A., Herdewijn, P., Hannaert, V., Michels, P. A. M., Opperdoes, F. R. & Hol, W. G. J. (1994a). Selective inhibition of trypanosomal glyceraldehyde-3-phosphate dehydrogenase by protein structure-based design: toward new drugs for the treatment of sleeping sickness. J. Med. Chem. 37, 3605-3613.
    • (1994) J. Med. Chem. , vol.37 , pp. 3605-3613
    • Verlinde, C.L.M.J.1    Callens, M.2    Van Calenbergh, S.3    Van Aerschot, A.4    Herdewijn, P.5    Hannaert, V.6    Michels, P.A.M.7    Opperdoes, F.R.8    Hol, W.G.J.9
  • 39
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R. K., Terpstra, P. & Hol, W. G. J. (1986). Prediction of the occurrence of the ADP-binding βαβ fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187, 101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 40
    • 13144252338 scopus 로고
    • On the treatment of protein data measured on the oscillation camera
    • Wilson, K. & Yeates, D. (1979). On the treatment of protein data measured on the oscillation camera. Acta Crystallog. sect. A, 35, 146-157.
    • (1979) Acta Crystallog. Sect. A , vol.35 , pp. 146-157
    • Wilson, K.1    Yeates, D.2
  • 41
    • 0022803106 scopus 로고
    • Distribution of the pentose phosphate pathway in living organisms
    • Wood, T. (1986). Distribution of the pentose phosphate pathway in living organisms. Cell Biochem. Funct. 4, 235-240.
    • (1986) Cell Biochem. Funct. , vol.4 , pp. 235-240
    • Wood, T.1
  • 42
    • 0030045604 scopus 로고    scopus 로고
    • The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 Å resolution
    • Zhang, Y., Bond, C. S., Bailey, S., Cunningham, M. L., Fairlamb, A. H. & Hunter, W. N. (1996). The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 Å resolution. Protein Sci. 5, 52-61.
    • (1996) Protein Sci. , vol.5 , pp. 52-61
    • Zhang, Y.1    Bond, C.S.2    Bailey, S.3    Cunningham, M.L.4    Fairlamb, A.H.5    Hunter, W.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.