메뉴 건너뛰기




Volumn 12, Issue 1, 2004, Pages 41-53

The Crystal Structure of Trypanosoma cruzi dUTPase Reveals a Novel dUTP/dUDP Binding Fold

Author keywords

[No Author keywords available]

Indexed keywords

2 DEOXYURIDINE DIPHOSPHATE; DEOXYURIDINE DERIVATIVE; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; DIMER; ENZYME; NUCLEOTIDE; PYROPHOSPHORIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

EID: 1642575114     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.11.016     Document Type: Article
Times cited : (62)

References (41)
  • 2
    • 0007000046 scopus 로고
    • Synthesis of deoxyribonucleoside diphosphates with enzymes from Escherichia coli
    • Bertani L.E., Haggmark A., Reichard P. Synthesis of deoxyribonucleoside diphosphates with enzymes from Escherichia coli. J. Biol. Chem. 236:1961;PC67-PC68.
    • (1961) J. Biol. Chem. , vol.236
    • Bertani, L.E.1    Haggmark, A.2    Reichard, P.3
  • 4
    • 0034652380 scopus 로고    scopus 로고
    • Properties of Leishmania major dUTP nucleotidohydrolase, a distinct nucleotide-hydrolysing enzyme in kinetoplastids
    • Camacho A., Hidalgo-Zarco F., Bernier-Villamor V., Ruiz-Perez L.M., Gonzalez-Pacanowska D. Properties of Leishmania major dUTP nucleotidohydrolase, a distinct nucleotide-hydrolysing enzyme in kinetoplastids. Biochem. J. 346:2000;163-168.
    • (2000) Biochem. J. , vol.346 , pp. 163-168
    • Camacho, A.1    Hidalgo-Zarco, F.2    Bernier-Villamor, V.3    Ruiz-Perez, L.M.4    Gonzalez-Pacanowska, D.5
  • 5
    • 0028103275 scopus 로고
    • Collaborative Computational Project 4) the CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 6
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan K.D., Zhang K.Y. Density modification for macromolecular phase improvement. Prog. Biophys. Mol. Biol. 72:1999;245-270.
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 7
    • 0023967987 scopus 로고
    • Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli
    • el-Hajj H.H., Zhang H., Weiss B. Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli. J. Bacteriol. 170:1988;1069-1075.
    • (1988) J. Bacteriol. , vol.170 , pp. 1069-1075
    • El-Hajj, H.H.1    Zhang, H.2    Weiss, B.3
  • 8
    • 0032541311 scopus 로고    scopus 로고
    • Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection
    • Engel J.C., Doyle P.S., Hsieh I., McKerrow J.H. Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection. J. Exp. Med. 188:1998;725-734.
    • (1998) J. Exp. Med. , vol.188 , pp. 725-734
    • Engel, J.C.1    Doyle, P.S.2    Hsieh, I.3    McKerrow, J.H.4
  • 9
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced colouring capabilities
    • Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced colouring capabilities. J. Mol. Graph. 15:1997;133-138.
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 10
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D. 55:1999;938-940.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 11
    • 0003481596 scopus 로고
    • Stereochemistry of enzymatic reactions
    • New York: W.H. Freeman and Company
    • Fersht, A. (1985). Stereochemistry of enzymatic reactions. In Enzyme Structure and Mechanism (New York: W.H. Freeman and Company), pp. 221-247.
    • (1985) Enzyme Structure and Mechanism , pp. 221-247
    • Fersht, A.1
  • 12
    • 0027426749 scopus 로고
    • DUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae
    • Gadsden M.H., McIntosh E.M., Game J.C., Wilson P.J., Haynes R.H. dUTP pyrophosphatase is an essential enzyme in Saccharomyces cerevisiae. EMBO J. 12:1993;4425-4431.
    • (1993) EMBO J. , vol.12 , pp. 4425-4431
    • Gadsden, M.H.1    McIntosh, E.M.2    Game, J.C.3    Wilson, P.J.4    Haynes, R.H.5
  • 13
  • 14
  • 18
    • 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
  • 19
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure. pattern recognition of hydrogen-bonded and geometrical features Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 20
    • 0029820083 scopus 로고    scopus 로고
    • Kinetic characterization of dUTPase from Escherichia coli
    • Larsson G., Nyman P.O., Kvassman J.O. Kinetic characterization of dUTPase from Escherichia coli. J. Biol. Chem. 271:1996;24010-24016.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24010-24016
    • Larsson, G.1    Nyman, P.O.2    Kvassman, J.O.3
  • 22
    • 0025293893 scopus 로고
    • Protein sequence comparisons show that the "pseudoproteases" encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family
    • McGeoch D.J. Protein sequence comparisons show that the "pseudoproteases" encoded by poxviruses and certain retroviruses belong to the deoxyuridine triphosphatase family. Nucleic Acids Res. 18:1990;4105-4110.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4105-4110
    • McGeoch, D.J.1
  • 23
    • 0028057108 scopus 로고
    • Raster3d Version-2.0: A program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E.P. Raster3d Version-2.0. a program for photorealistic molecular graphics Acta Crystallogr. D. 50:1994;869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 24
    • 0030587564 scopus 로고    scopus 로고
    • Human dUTP pyrophosphatase: Uracil recognition by a beta hairpin and active sites formed by three separate subunits
    • Mol C.D., Harris J.M., McIntosh E.M., Tainer J.A. Human dUTP pyrophosphatase. uracil recognition by a beta hairpin and active sites formed by three separate subunits Structure. 4:1996;1077-1092.
    • (1996) Structure , vol.4 , pp. 1077-1092
    • Mol, C.D.1    Harris, J.M.2    McIntosh, E.M.3    Tainer, J.A.4
  • 25
    • 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. D. 53:1997;240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 26
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • J.C.W. Carter, & R.M. Sweet. New York: Academic Press
    • Navaza J., Saludjian P. AMoRe. an automated molecular replacement program package Carter J.C.W., Sweet R.M. Methods in Enzymology. 1997;581-594 Academic Press, New York.
    • (1997) Methods in Enzymology , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 27
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • J.C.W. Carter, & R.M. Sweet. New York: Academic Press
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Carter J.C.W., Sweet R.M. Methods in Enzymology. 1997;307-326 Academic Press, New York.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 19144373027 scopus 로고    scopus 로고
    • The problem with pyrimidines
    • Pearl L.H., Savva R. The problem with pyrimidines. Nat. Struct. Biol. 3:1996;485-487.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 485-487
    • Pearl, L.H.1    Savva, R.2
  • 31
    • 0034744964 scopus 로고    scopus 로고
    • Homotrimeric dUTPases; Structural solutions for specific recognition and hydrolysis of dUTP
    • Persson R., Cedergren-Zeppezauer E., Wilson K.S. Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP. Curr. Protein Pept. Sci. 2:2001;287-300.
    • (2001) Curr. Protein Pept. Sci , vol.2 , pp. 287-300
    • Persson, R.1    Cedergren-Zeppezauer, E.2    Wilson, K.S.3
  • 33
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan V., Finch J.T., Graziano V., Lee P.L., Sweet R.M. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. Nature. 362:1993;219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 34
  • 36
    • 0030716497 scopus 로고    scopus 로고
    • Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
    • Rittinger K., Walker P.A., Eccleston J.F., Smerdon S.J., Gamblin S.J. Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature. 389:1997;758-762.
    • (1997) Nature , vol.389 , pp. 758-762
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Smerdon, S.J.4    Gamblin, S.J.5
  • 37
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz G.E. Binding of nucleotides by proteins. Curr. Opin. Struct. Biol. 2:1992;61-67.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 38
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang S.R. G protein mechanisms. insights from structural analysis Annu. Rev. Biochem. 66:1997;639-678.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 40
    • 0027968068 scopus 로고
    • Clustal w: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. Clustal w. improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.