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Volumn 11, Issue 1, 2003, Pages 31-42

Structure of Escherichia coli ribose-5-phosphate isomerase: A ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle

Author keywords

Arabinose 5 phosphate; Calvin cycle; MAD; Pentose phosphate pathway; Ribose 5 phosphate isomerase; X ray crystallography

Indexed keywords

ALCOHOL DEHYDROGENASE; BACTERIAL ENZYME; CARBOHYDRATE; ISOMERASE; PENTOSE PHOSPHATE; RIBOSE 5 PHOSPHATE; RIBULOSE PHOSPHATE;

EID: 0037224131     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00933-4     Document Type: Article
Times cited : (101)

References (36)
  • 1
    • 0014323155 scopus 로고
    • Improved Sephadex procedures for buffer exchange of ribosephosphate isomerase
    • Knowles F.C., Pon N.G. Improved Sephadex procedures for buffer exchange of ribosephosphate isomerase. Anal. Biochem. 24:1968;305-313.
    • (1968) Anal. Biochem. , vol.24 , pp. 305-313
    • Knowles, F.C.1    Pon, N.G.2
  • 2
    • 0034650538 scopus 로고    scopus 로고
    • D-ribose-5-phosphate isomerase from spinach: Heterologous overexpression, purification, characterization, and site-directed mutagenesis of the recombinant enzyme
    • Jung C.H., Hartman F.C., Lu T.Y., Larimer F.W. D-ribose-5-phosphate isomerase from spinach. heterologous overexpression, purification, characterization, and site-directed mutagenesis of the recombinant enzyme Arch. Biochem. Biophys. 373:2000;409-417.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 409-417
    • Jung, C.H.1    Hartman, F.C.2    Lu, T.Y.3    Larimer, F.W.4
  • 4
    • 0030060223 scopus 로고    scopus 로고
    • Ribose catabolism of Escherichia coli: Characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression
    • Sorensen K.I., Hove-Jensen B. Ribose catabolism of Escherichia coli. characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression J. Bacteriol. 178:1996;1003-1011.
    • (1996) J. Bacteriol. , vol.178 , pp. 1003-1011
    • Sorensen, K.I.1    Hove-Jensen, B.2
  • 5
    • 0016784251 scopus 로고
    • Two ribose-5-phosphate isomerases from Escherichia coli K12: Partial characterisation of the enzymes and consideration of their possible physiological roles
    • Essenberg M.K., Cooper R.A. Two ribose-5-phosphate isomerases from Escherichia coli K12. partial characterisation of the enzymes and consideration of their possible physiological roles Eur. J. Biochem. 55:1975;323-332.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 323-332
    • Essenberg, M.K.1    Cooper, R.A.2
  • 6
    • 0036278183 scopus 로고    scopus 로고
    • A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure
    • Ishikawa K., Matsui I., Payan F., Cambillau C., Ishida H., Kawarabayasi Y., Kikuchi H., Roussel A. A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure. Structure. 10:2002;877-886.
    • (2002) Structure , vol.10 , pp. 877-886
    • Ishikawa, K.1    Matsui, I.2    Payan, F.3    Cambillau, C.4    Ishida, H.5    Kawarabayasi, Y.6    Kikuchi, H.7    Roussel, A.8
  • 7
    • 0027199219 scopus 로고
    • Escherichia coli rpiA gene encoding ribose phosphate isomerase A
    • Hove-Jensen B., Maigaard M. Escherichia coli rpiA gene encoding ribose phosphate isomerase A. J. Bacteriol. 175:1993;5628-5635.
    • (1993) J. Bacteriol. , vol.175 , pp. 5628-5635
    • Hove-Jensen, B.1    Maigaard, M.2
  • 9
    • 0014934376 scopus 로고
    • Spinach 5-phosphoribose isomerase. Purification and properties of the enzyme
    • Rutner A.C. Spinach 5-phosphoribose isomerase. Purification and properties of the enzyme. Biochemistry. 9:1970;178-184.
    • (1970) Biochemistry , vol.9 , pp. 178-184
    • Rutner, A.C.1
  • 11
    • 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. 233:1993;123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 12
    • 0018786880 scopus 로고
    • Inhibition of ribose-5-phosphate isomerase by 4-phosphoerythronate
    • Woodruff W.W. III, Wolfenden R. Inhibition of ribose-5-phosphate isomerase by 4-phosphoerythronate. J. Biol. Chem. 254:1979;5866-5867.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5866-5867
    • Woodruff W.W. III1    Wolfenden, R.2
  • 14
    • 0035800048 scopus 로고    scopus 로고
    • Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate
    • Lee J.H., Chang K.Z., Patel V., Jeffery C.J. Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate. Biochemistry. 40:2001;7799-7805.
    • (2001) Biochemistry , vol.40 , pp. 7799-7805
    • Lee, J.H.1    Chang, K.Z.2    Patel, V.3    Jeffery, C.J.4
  • 16
    • 0032520213 scopus 로고    scopus 로고
    • Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution: Insights into a new family of kinase structures
    • Sigrell J.A., Cameron A.D., Jones T.A., Mowbray S.L. Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution. insights into a new family of kinase structures Structure. 6:1998;183-193.
    • (1998) Structure , vol.6 , pp. 183-193
    • Sigrell, J.A.1    Cameron, A.D.2    Jones, T.A.3    Mowbray, S.L.4
  • 17
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution
    • Lindqvist Y., Schneider G., Ermler U., Sundstrom M. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution. EMBO J. 11:1992;2373-2379.
    • (1992) EMBO J. , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundstrom, M.4
  • 18
    • 0014734211 scopus 로고
    • Spectrophotometric assay for D-ribose-5-phosphateketol-isomerase and for D-ribulose-5-phosphate 3-epimerase
    • Wood T. Spectrophotometric assay for D-ribose-5-phosphateketol-isomerase and for D-ribulose-5-phosphate 3-epimerase. Anal. Biochem. 33:1970;297-306.
    • (1970) Anal. Biochem. , vol.33 , pp. 297-306
    • Wood, T.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. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project 4) suite. programs for protein crystallography Acta Crystallogr. D50:1994;760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 23
    • 0030809260 scopus 로고    scopus 로고
    • WARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models
    • Perrakis A., Sixma T.K., Wilson K.S., Lamzin V.S. wARP. improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models Acta Crystallogr. D53:1997;448-455.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 448-455
    • Perrakis, A.1    Sixma, T.K.2    Wilson, K.S.3    Lamzin, V.S.4
  • 25
    • 0030589514 scopus 로고    scopus 로고
    • Phi/psi-cology: Ramachandran revisited
    • Kleywegt G.J., Jones T.A. Phi/psi-cology. Ramachandran revisited Structure. 4:1996;1395-1400.
    • (1996) Structure , vol.4 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 26
    • 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. 30:1997;1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 27
    • 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. Acta Crystallogr. D53:1997;240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 28
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., Richards F.M. The interpretation of protein structures. estimation of static accessibility J. Mol. Biol. 55:1971;379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 29
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • Kleywegt G.J. Use of non-crystallographic symmetry in protein structure refinement. Acta Crystallogr. D52:1996;842-857.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 842-857
    • Kleywegt, G.J.1
  • 30
    • 0030841589 scopus 로고    scopus 로고
    • Detecting folding motifs and similarities in protein structures
    • Kleywegt G.J., Jones T.A. Detecting folding motifs and similarities in protein structures. Methods Enzymol. 277:1997;525-545.
    • (1997) Methods Enzymol. , vol.277 , pp. 525-545
    • Kleywegt, G.J.1    Jones, T.A.2
  • 31
    • 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. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47:1991;110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 32
    • 0034479757 scopus 로고    scopus 로고
    • Top: A new method for protein structure comparisons and similarity searches
    • Lu G. Top. a new method for protein structure comparisons and similarity searches J. Appl. Crystallogr. 33:2000;176-183.
    • (2000) J. Appl. Crystallogr. , vol.33 , pp. 176-183
    • Lu, G.1
  • 33
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • Karplus K., Barrett C., Hughey R. Hidden Markov models for detecting remote protein homologies. Bioinformatics. 14:1998;846-856.
    • (1998) Bioinformatics , vol.14 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 34
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones T.A., Kjeldgaard M.O. Electron-density map interpretation. Methods Enzymol. 277:1997;173-208.
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.O.2
  • 35
    • 0034903751 scopus 로고    scopus 로고
    • Molray - A web interface between O and the POV-Ray ray tracer
    • Harris M., Jones T.A. Molray - a web interface between O and the POV-Ray ray tracer. Acta Crystallogr. D57:2001;1201-1203.
    • (2001) Acta Crystallogr. , vol.D57 , pp. 1201-1203
    • Harris, M.1    Jones, T.A.2
  • 36
    • 0028922586 scopus 로고
    • Ligplot: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., Thornton J.M. Ligplot. a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 8:1995;127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.