메뉴 건너뛰기




Volumn 43, Issue 40, 2004, Pages 12770-12779

X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; MONOMERS; OLIGOMERS; PROTEINS; SOLVENTS; SUBSTRATES; X RAY ANALYSIS; X RAY CRYSTALLOGRAPHY;

EID: 4944254297     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0490688     Document Type: Article
Times cited : (46)

References (42)
  • 1
    • 0028116826 scopus 로고
    • Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search
    • Koonin, E. V., and Tatusov, R. L. (1994) Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search, J. Mol. Biol. 244, 125-132.
    • (1994) J. Mol. Biol. , vol.244 , pp. 125-132
    • Koonin, E.V.1    Tatusov, R.L.2
  • 2
    • 0035940484 scopus 로고    scopus 로고
    • MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases
    • Selengut, J. D. (2001) MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases, Biochemistry 40, 12704-12711.
    • (2001) Biochemistry , vol.40 , pp. 12704-12711
    • Selengut, J.D.1
  • 3
    • 0029786674 scopus 로고    scopus 로고
    • Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An α/β hydrolase structure that is different from the α/β hydrolase fold
    • Hisano, T., Hata, Y., Fujii, T., Liu, J. Q., Kurihara, T., Esaki, N., and Soda, K. (1996) Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An α/β hydrolase structure that is different from the α/β hydrolase fold, J. Biol. Chem. 271, 20322-20330.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20322-20330
    • Hisano, T.1    Hata, Y.2    Fujii, T.3    Liu, J.Q.4    Kurihara, T.5    Esaki, N.6    Soda, K.7
  • 4
    • 0031455377 scopus 로고    scopus 로고
    • Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ 10 complexed with the substrate-analogue formate
    • Ridder, I. S., Rozeboom, H. J., Kalk, K. H., Janssen, D. B., and Dijkstra, B. W. (1997) Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ 10 complexed with the substrate-analogue formate, J. Biol. Chem. 272, 33015-33022.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33015-33022
    • Ridder, I.S.1    Rozeboom, H.J.2    Kalk, K.H.3    Janssen, D.B.4    Dijkstra, B.W.5
  • 5
    • 0037008092 scopus 로고    scopus 로고
    • Caught in the act: The structure of phosphorylated β- phosphoglucomutase from Lactococcus lactis
    • Lahiri, S. D., Zhang, G., Dunaway-Mariano, D., and Allen, K. N. (2002) Caught in the act: the structure of phosphorylated β-phosphoglucomutase from Lactococcus lactis, Biochemistry 41, 8351-8359.
    • (2002) Biochemistry , vol.41 , pp. 8351-8359
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 6
    • 0034730072 scopus 로고    scopus 로고
    • The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: Insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily
    • Morais, M. C., Zhang, W., Baker, A. S., Zhang, G., Dunaway-Mariano, D., and Allen, K. N. (2000) The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily, Biochemistry 39, 10385-10396.
    • (2000) Biochemistry , vol.39 , pp. 10385-10396
    • Morais, M.C.1    Zhang, W.2    Baker, A.S.3    Zhang, G.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 7
    • 0035155638 scopus 로고    scopus 로고
    • Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 Å resolution
    • Wang, W., Kim, R., Jancarik, J., Yokota, H., and Kim, S. H. (2001) Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 Å resolution, Structure 9, 65-71.
    • (2001) Structure , vol.9 , pp. 65-71
    • Wang, W.1    Kim, R.2    Jancarik, J.3    Yokota, H.4    Kim, S.H.5
  • 8
    • 0036301579 scopus 로고    scopus 로고
    • Structural characterization of the reaction pathway in phosphoserine phosphatase: Crystallographic "snapshots" of intermediate states
    • Wang, W., Cho, H. S., Kim, R., Jancarik, J., Yokota, H., Nguyen, H. H., Grigoriev, I. V., Wemmer, D. E., and Kim, S. H. (2002) Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states, J. Mol. Biol. 319, 421-431.
    • (2002) J. Mol. Biol. , vol.319 , pp. 421-431
    • Wang, W.1    Cho, H.S.2    Kim, R.3    Jancarik, J.4    Yokota, H.5    Nguyen, H.H.6    Grigoriev, I.V.7    Wemmer, D.E.8    Kim, S.H.9
  • 9
    • 0032724654 scopus 로고    scopus 로고
    • Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase
    • Ridder, I. S., Rozeboom, H. J., Kalk, K. H., and Dijkstra, B. W. (1999) Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase, J. Biol. Chem. 274, 30672-30678.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30672-30678
    • Ridder, I.S.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 10
    • 0036711227 scopus 로고    scopus 로고
    • Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase
    • Galburt, E. A., Pelletier, J., Wilson, G., and Stoddard, B. L. (2002) Structure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase, Structure 10, 1249-1260.
    • (2002) Structure , vol.10 , pp. 1249-1260
    • Galburt, E.A.1    Pelletier, J.2    Wilson, G.3    Stoddard, B.L.4
  • 11
    • 0036499628 scopus 로고    scopus 로고
    • From structure to function: YrbI from Haemophilus influenzae (HI1679) is a phosphatase
    • Parsons, J. F., Lim, K., Tempczyk, A., Krajewski, W., Eisenstein, E., and Herzberg, O. (2002) From structure to function: YrbI from Haemophilus influenzae (HI1679) is a phosphatase, Proteins 46, 393-404.
    • (2002) Proteins , vol.46 , pp. 393-404
    • Parsons, J.F.1    Lim, K.2    Tempczyk, A.3    Krajewski, W.4    Eisenstein, E.5    Herzberg, O.6
  • 12
    • 0038719689 scopus 로고    scopus 로고
    • Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
    • Wu, J., and Woodard, R. W. (2003) Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, J. Biol. Chem. 278, 18117-18123.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18117-18123
    • Wu, J.1    Woodard, R.W.2
  • 13
    • 0034682618 scopus 로고    scopus 로고
    • MDP-1: A novel eukaryotic magnesium-dependent phosphatase
    • Selengut, J. D., and Levine, R. L. (2000) MDP-1: A novel eukaryotic magnesium-dependent phosphatase, Biochemistry 39, 8315-8324.
    • (2000) Biochemistry , vol.39 , pp. 8315-8324
    • Selengut, J.D.1    Levine, R.L.2
  • 14
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • Barford, D., Das, A. K., and Egloff, M. P. (1998) The structure and mechanism of protein phosphatases: insights into catalysis and regulation, Annu. Rev. Biophys. Biomol. Struct. 27, 133-164.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 15
    • 0028880718 scopus 로고
    • Protein tyrosine phosphatases take off
    • Barford, D., Jia, Z., and Tonks, N. K. (1995) Protein tyrosine phosphatases take off, Nat. Struct. Biol. 2, 1043-1053.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1043-1053
    • Barford, D.1    Jia, Z.2    Tonks, N.K.3
  • 16
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 17
    • 0031058188 scopus 로고    scopus 로고
    • (Carter, C. W., Jr. and Sweet, R. M., Ed.), Academic Press, New York
    • de La Fortelle, E., and Bricogne, G. (1997) in Methods in Enzymology (Carter, C. W., Jr. and Sweet, R. M., Ed.) pp 472-494, Academic Press, New York.
    • (1997) Methods in Enzymology , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 18
    • 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., and Kjeldgaard, G. J. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47 (Part 2), 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, G.J.4
  • 20
    • 0031569392 scopus 로고    scopus 로고
    • New applications of simulated annealing in X-ray crystallography and solution NMR
    • Brünger, A. T., Adams, P. D., and Rice, L. M. (1997) New applications of simulated annealing in X-ray crystallography and solution NMR, Structure 5, 325-336.
    • (1997) Structure , vol.5 , pp. 325-336
    • Brünger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 21
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis, I. W., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2004) MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes, Nucleic Acids Res. 32, W615-W619.
    • (2004) Nucleic Acids Res. , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 22
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin, A., and Teplyakov, A. (2000) An approach to multi-copy search in molecular replacement, Acta Crystallogr. D56 (Part 12), 1622-1624.
    • (2000) Acta Crystallogr. , vol.D56 , Issue.PART 12 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 24
    • 0029083530 scopus 로고
    • The turning point in genome research
    • Boguski, M. S. (1995) The turning point in genome research, Trends Biochem. Sci. 20, 295-296.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 295-296
    • Boguski, M.S.1
  • 26
    • 0030765455 scopus 로고    scopus 로고
    • Dali/FSSP classification of three-dimensional protein folds
    • Holm, L., and Sander, C. (1997) Dali/FSSP classification of three-dimensional protein folds, Nucleic Acids Res. 25, 231-234.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 231-234
    • Holm, L.1    Sander, C.2
  • 27
    • 0032849109 scopus 로고    scopus 로고
    • Detoxification of environmental mutagens and carcinogens: Structure, mechanism, and evolution of liver epoxide hydrolase
    • Argiriadi, M. A., Morisseau, C., Hammock, B. D., and Christianson, D. W. (1999) Detoxification of environmental mutagens and carcinogens: structure, mechanism, and evolution of liver epoxide hydrolase, Proc. Natl. Acad. Sci. U.S.A. 96, 10637-10642.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10637-10642
    • Argiriadi, M.A.1    Morisseau, C.2    Hammock, B.D.3    Christianson, D.W.4
  • 28
    • 0037452577 scopus 로고    scopus 로고
    • The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity
    • Newman, J. W., Morisseau, C., Harris, T. R., and Hammock, B. D. (2003) The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity, Proc. Natl. Acad. Sci. U.S.A. 100, 1558-1563.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 1558-1563
    • Newman, J.W.1    Morisseau, C.2    Harris, T.R.3    Hammock, B.D.4
  • 30
    • 85069016834 scopus 로고    scopus 로고
    • The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction
    • Lahiri, S. D., Zhang, G., Dunaway-Mariano, D., and Allen, K. N. (2003) The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction, Science 108, 2710.
    • (2003) Science , vol.108 , pp. 2710
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 32
    • 0037069406 scopus 로고    scopus 로고
    • Kinetic Evidence for a Substrate-Induced Fit in Phosphonoacetaldehyde Hydrolase Catalysis
    • Zhang, G., Mazurkie, A. S., Dunaway-Mariano, D., and Allen, K. N. (2002) Kinetic Evidence for a Substrate-Induced Fit in Phosphonoacetaldehyde Hydrolase Catalysis, Biochemistry 41, 13370-13377.
    • (2002) Biochemistry , vol.41 , pp. 13370-13377
    • Zhang, G.1    Mazurkie, A.S.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 33
    • 0037154845 scopus 로고    scopus 로고
    • Generality of solvation effects on the hydrolysis rates of phosphate monoesters and their possible relevance to enzymatic catalysis
    • Grzyska, P. K., Czyryca, P. G., Golightly, J., Small, K., Larsen, P., Hoff, R. H., and Hengge, A. C. (2002) Generality of solvation effects on the hydrolysis rates of phosphate monoesters and their possible relevance to enzymatic catalysis, J. Org. Chem. 67, 1214-1220.
    • (2002) J. Org. Chem. , vol.67 , pp. 1214-1220
    • Grzyska, P.K.1    Czyryca, P.G.2    Golightly, J.3    Small, K.4    Larsen, P.5    Hoff, R.H.6    Hengge, A.C.7
  • 34
    • 0021049880 scopus 로고
    • Waterlogged molecules
    • Wolfenden, R. (1983) Waterlogged molecules, Science 222, 1087-1093.
    • (1983) Science , vol.222 , pp. 1087-1093
    • Wolfenden, R.1
  • 35
    • 0032538627 scopus 로고    scopus 로고
    • Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites
    • Warshel, A. (1998) Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites, J. Biol. Chem. 273, 27035-27038.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27035-27038
    • Warshel, A.1
  • 37
    • 0032555658 scopus 로고    scopus 로고
    • Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity
    • Zhang, M., Stauffacher, C. V., Lin, D., and Van Etten, R. L. (1998) Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. Implications for substrate specificity, J. Biol. Chem. 273, 21714-21720.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21714-21720
    • Zhang, M.1    Stauffacher, C.V.2    Lin, D.3    Van Etten, R.L.4
  • 38
    • 0035844140 scopus 로고    scopus 로고
    • Distinct binding determinants for ERK2/p38α and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1
    • Slack, D. N., Setemes, O. M., Gabrielsen, M., and Keyse, S. M. (2001) Distinct binding determinants for ERK2/p38α and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1, J. Biol. Chem. 276, 16491-16500.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16491-16500
    • Slack, D.N.1    Setemes, O.M.2    Gabrielsen, M.3    Keyse, S.M.4
  • 40
    • 4344585269 scopus 로고    scopus 로고
    • Phosphoryl group transfer: Evolution of a catalytic scaffold
    • Allen, K. N., and Dunaway-Mariano, D. (2004) Phosphoryl group transfer: evolution of a catalytic scaffold, Trends Biochem. Sci. 29, 495-503.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 495-503
    • Allen, K.N.1    Dunaway-Mariano, D.2
  • 41
    • 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. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.