메뉴 건너뛰기




Volumn 126, Issue 2, 2003, Pages 173-180

High-resolution crystal structure of Trypanosoma brucei UDP-galactose 4′-epimerase: A potential target for structure-based development of novel trypanocides

Author keywords

Epimerase; Galactose; Trypanosoma brucei; UDP Gal; X ray structure

Indexed keywords

ANTITRYPANOSOMAL AGENT; CYSTINE; GLYCINE; NICOTINAMIDE ADENINE DINUCLEOTIDE; URIDINE DIPHOSPHATE; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE;

EID: 0037327814     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(02)00243-8     Document Type: Article
Times cited : (49)

References (31)
  • 1
    • 0037197847 scopus 로고    scopus 로고
    • Galactose metabolism is essential for the African sleeping sickness parasite Trypanosoma brucei
    • Roper J.R., Guther M.L.S., Milne K.G., Ferguson M.A.J. Galactose metabolism is essential for the African sleeping sickness parasite Trypanosoma brucei. Proc. Natl. Acad. Sci. U.S.A. 99:2002;5884-5889.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5884-5889
    • Roper, J.R.1    Guther, M.L.S.2    Milne, K.G.3    Ferguson, M.A.J.4
  • 3
    • 0032029271 scopus 로고    scopus 로고
    • The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei
    • Mehlert A., Zitzmann N., Richardson J.M., Treumann A., Ferguson M.A.J. The glycosylation of the variant surface glycoproteins and procyclic acidic repetitive proteins of Trypanosoma brucei. Mol. Biochem. Parasitol. 91:1998;145-152.
    • (1998) Mol. Biochem. Parasitol. , vol.91 , pp. 145-152
    • Mehlert, A.1    Zitzmann, N.2    Richardson, J.M.3    Treumann, A.4    Ferguson, M.A.J.5
  • 4
    • 0033592539 scopus 로고    scopus 로고
    • N-linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei
    • Nolan D.P., Geuskens M., Pays E. N-linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei. Curr. Biol. 9:1999;1169-1172.
    • (1999) Curr. Biol. , vol.9 , pp. 1169-1172
    • Nolan, D.P.1    Geuskens, M.2    Pays, E.3
  • 5
    • 0029920614 scopus 로고    scopus 로고
    • The Leloir pathway: A mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose
    • Frey P.A. The Leloir pathway: a mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose. FASEB J. 10:1996;461-470.
    • (1996) FASEB J. , vol.10 , pp. 461-470
    • Frey, P.A.1
  • 7
    • 0030458319 scopus 로고    scopus 로고
    • The fascinating complexities of steroid-binding enzymes
    • Duax W.L., Griffin J.F., Ghosh D. The fascinating complexities of steroid-binding enzymes. Curr. Opin. Struct. Biol. 6:1996;813-823.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 813-823
    • Duax, W.L.1    Griffin, J.F.2    Ghosh, D.3
  • 8
    • 0032544212 scopus 로고    scopus 로고
    • Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from E. coli
    • Thoden J.B., Holden H.M. Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from E. coli. Biochemistry. 37:1998;11469-11477.
    • (1998) Biochemistry , vol.37 , pp. 11469-11477
    • Thoden, J.B.1    Holden, H.M.2
  • 9
    • 0034673977 scopus 로고    scopus 로고
    • Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase
    • Thoden J.B., Wohlers T.M., Fridovich-Keil J.L., Holden H.M. Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase. Biochemistry. 39:2000;5691-5701.
    • (2000) Biochemistry , vol.39 , pp. 5691-5701
    • Thoden, J.B.1    Wohlers, T.M.2    Fridovich-Keil, J.L.3    Holden, H.M.4
  • 11
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 12
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 13
    • 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
  • 14
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr 1994;D50:760-73.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-773
  • 15
    • 84920325457 scopus 로고
    • AMoRe: An automated molecular replacement program package
    • Navaza J. AMoRe: an automated molecular replacement program package. Acta Crystallogr. A50:1994;157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 17
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A32:1976;922-923.
    • (1976) Acta Crystallogr. , vol.A32 , pp. 922-923
    • Kabsch, W.1
  • 18
    • 84889120137 scopus 로고
    • 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. 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
  • 20
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation - The free R value - Methods and applications
    • Brünger A.T. Assessment of phase accuracy by cross validation - the free R value - methods and applications. Acta Crystallogr. D49:1993;24-36.
    • (1993) Acta Crystallogr. , vol.D49 , pp. 24-36
    • Brünger, A.T.1
  • 22
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt G.J., Jones T.A. Efficient rebuilding of protein structures. Acta Crystallogr. D52:1996;829-832.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 23
    • 0024297278 scopus 로고
    • Biosynthesis of a variant surface glycoprotein of Trypanosoma brucei
    • Bangs J.D., Doering T.L., Englund P.T., Hart G.W. Biosynthesis of a variant surface glycoprotein of Trypanosoma brucei. J. Biol. Chem. 263:1988;17697-17705.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17697-17705
    • Bangs, J.D.1    Doering, T.L.2    Englund, P.T.3    Hart, G.W.4
  • 24
    • 0026570234 scopus 로고
    • Galactose-containing glycosylphosphatidylinositols in Trypanosoma brucei
    • Mayor S., Menon A.K., Cross G.A.M. Galactose-containing glycosylphosphatidylinositols in Trypanosoma brucei. J. Biol. Chem. 267:1992;754-761.
    • (1992) J. Biol. Chem. , vol.267 , pp. 754-761
    • Mayor, S.1    Menon, A.K.2    Cross, G.A.M.3
  • 25
    • 0032571308 scopus 로고    scopus 로고
    • Structure of the glycosylphosphatidylinositol membrane anchor glycan of a class-2 variant surface glycoprotein from Trypanosoma brucei
    • Mehlert A., Richardson J.M., Ferguson M.A.J. Structure of the glycosylphosphatidylinositol membrane anchor glycan of a class-2 variant surface glycoprotein from Trypanosoma brucei. J. Mol. Biol. 277:1998;379-392.
    • (1998) J. Mol. Biol. , vol.277 , pp. 379-392
    • Mehlert, A.1    Richardson, J.M.2    Ferguson, M.A.J.3
  • 26
    • 1542563485 scopus 로고
    • Evolutionary and structural relationships among dehydrogenases
    • Boyer PD, editor. New York (USA): Academic Press
    • Rossmann MG, Liljas A, Brändén C-I, Banaszak LJ. Evolutionary and structural relationships among dehydrogenases. In: Boyer PD, editor. The enzymes, vol. 11. 3rd ed. New York (USA): Academic Press; 1975. p. 61-102.
    • (1975) The Enzymes. 3rd Ed. , vol.11 , pp. 61-102
    • Rossmann, M.G.1    Liljas, A.2    Brändén, C.-I.3    Banaszak, L.J.4
  • 27
    • 0030832007 scopus 로고    scopus 로고
    • Mechanistic roles of tyrosine149 and serine124 in UDP-galactose 4-epimerase from E. coli
    • Liu Y., Thoden J.B., Kim J., Berger E., Gulick A.M., Ruzicka F.J.et al. Mechanistic roles of tyrosine149 and serine124 in UDP-galactose 4-epimerase from E. coli. Biochemistry. 36:1997;10675-10684.
    • (1997) Biochemistry , vol.36 , pp. 10675-10684
    • Liu, Y.1    Thoden, J.B.2    Kim, J.3    Berger, E.4    Gulick, A.M.5    Ruzicka, F.J.6
  • 29
    • 0026244229 scopus 로고
    • MOLSCRIPT, a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT, a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0028057108 scopus 로고
    • Raster3d, a program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E.P. Raster3d, a program for photorealistic molecular graphics. Acta Crystallogr. D50:1994;869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 31
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.