메뉴 건너뛰기




Volumn 193, Issue 13, 2011, Pages 3175-3185

The Nudix hydrolase CDP-chase, a CDP-choline pyrophosphatase, is an asymmetric dimer with two distinct enzymatic activities

Author keywords

[No Author keywords available]

Indexed keywords

CDP CHASE PROTEIN; CITICOLINE; EXONUCLEASE; NUDIX HYDROLASE; UNCLASSIFIED DRUG;

EID: 79959362108     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00089-11     Document Type: Article
Times cited : (11)

References (47)
  • 2
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • Ames, B. N., and D. T. Dubin. 1960. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J. Biol. Chem. 235:769-775.
    • (1960) J. Biol. Chem. , vol.235 , pp. 769-775
    • Ames, B.N.1    Dubin, D.T.2
  • 3
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed "housecleaning" enzymes
    • Bessman, M. J., D. N. Frick, and S. F. O'Handley. 1996. The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. J. Biol. Chem. 271:25059-25062.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 4
    • 0034693059 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae PCD1 gene encodes a peroxisomal nudix hydrolase active toward coenzyme A and its derivatives
    • Cartwright, J. L., L. Gasmi, D. G. Spiller, and A. G. McLennan. 2000. The Saccharomyces cerevisiae PCD1 gene encodes a peroxisomal nudix hydrolase active toward coenzyme A and its derivatives. J. Biol. Chem. 275:32925-32930.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32925-32930
    • Cartwright, J.L.1    Gasmi, L.2    Spiller, D.G.3    McLennan, A.G.4
  • 5
    • 0028103275 scopus 로고
    • The CCP4 Suite-programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project, Number 4. 1994. The CCP4 Suite-programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 6
    • 45549083224 scopus 로고    scopus 로고
    • Crystal structure of the 25 kDa subunit of human cleavage factor Im
    • Coseno, M., et al. 2008. Crystal structure of the 25 kDa subunit of human cleavage factor Im. Nucleic Acids Res. 36:3474-3483.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 3474-3483
    • Coseno, M.1
  • 7
    • 38349117689 scopus 로고    scopus 로고
    • The bacterial enzyme RppH triggers messenger RNA degradation by 5' pyrophosphate removal
    • Deana, A., H. Celesnik, and J. G. Belasco. 2008. The bacterial enzyme RppH triggers messenger RNA degradation by 5' pyrophosphate removal. Nature 451:355-358.
    • (2008) Nature , vol.451 , pp. 355-358
    • Deana, A.1    Celesnik, H.2    Belasco, J.G.3
  • 8
    • 1842613501 scopus 로고    scopus 로고
    • Regulation of endospore formation in Bacillus subtilis
    • Errington, J. 2003. Regulation of endospore formation in Bacillus subtilis. Nat. Rev. Microbiol. 1:117-126.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 117-126
    • Errington, J.1
  • 9
    • 0033863915 scopus 로고    scopus 로고
    • Phosphocholine of pneumococcal teichoic acids: role in bacterial physiology and pneumococcal infection
    • Fischer, W. 2000. Phosphocholine of pneumococcal teichoic acids: role in bacterial physiology and pneumococcal infection. Res. Microbiol. 151:421-427.
    • (2000) Res. Microbiol. , vol.151 , pp. 421-427
    • Fischer, W.1
  • 10
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske, C. H., and Y. Subbarow. 1925. The colorimetric determination of phosphorus. J. Biol. Chem. 66:375-400.
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 11
    • 0035026968 scopus 로고    scopus 로고
    • The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family
    • Gabelli, S. B., M. A. Bianchet, M. J. Bessman, and L. M. Amzel. 2001. The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family. Nat. Struct. Biol. 8:467-472.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 467-472
    • Gabelli, S.B.1    Bianchet, M.A.2    Bessman, M.J.3    Amzel, L.M.4
  • 12
    • 0037199445 scopus 로고    scopus 로고
    • Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase
    • Gabelli, S. B., et al. 2002. Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase. Biochemistry 41:9279-9285.
    • (2002) Biochemistry , vol.41 , pp. 9279-9285
    • Gabelli, S.B.1
  • 13
    • 34547657390 scopus 로고    scopus 로고
    • Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis
    • Gabelli, S. B., et al. 2007. Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Structure 15:1014-1022.
    • (2007) Structure , vol.15 , pp. 1014-1022
    • Gabelli, S.B.1
  • 14
    • 67649986228 scopus 로고    scopus 로고
    • Structure and function of an ADP-ribose-dependent transcriptional regulator of NAD metabolism
    • Huang, N., et al. 2009. Structure and function of an ADP-ribose-dependent transcriptional regulator of NAD metabolism. Structure 17:939-951.
    • (2009) Structure , vol.17 , pp. 939-951
    • Huang, N.1
  • 15
    • 38949157741 scopus 로고    scopus 로고
    • Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism
    • Huang, N., et al. 2008. Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism. Structure 16:196-209.
    • (2008) Structure , vol.16 , pp. 196-209
    • Huang, N.1
  • 16
    • 33947716119 scopus 로고    scopus 로고
    • A semiempirical free energy force field with charge-based desolvation
    • Huey, R., G. M. Morris, A. J. Olson, and D. S. Goodsell. 2007. A semiempirical free energy force field with charge-based desolvation. J. Comput. Chem. 28:1145-1152.
    • (2007) J. Comput. Chem. , vol.28 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 17
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones, T. A., and M. Kjeldgaard. 1997. Electron-density map interpretation. Methods Enzymol. 277:173-208.
    • (1997) Methods Enzymol , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.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., J. Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47(Pt. 2):110-119.
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0043133626 scopus 로고    scopus 로고
    • Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis
    • Kang, L. W., S. B. Gabelli, J. E. Cunningham, S. F. O'Handley, and L. M. Amzel. 2003. Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis. Structure 11:1015-1023.
    • (2003) Structure , vol.11 , pp. 1015-1023
    • Kang, L.W.1    Gabelli, S.B.2    Cunningham, J.E.3    O'Handley, S.F.4    Amzel, L.M.5
  • 20
    • 55749086392 scopus 로고    scopus 로고
    • Dinucleotidesensing proteins: linking signaling networks and regulating transcription
    • Lamb, H. K., D. K. Stammers, and A. R. Hawkins. 2008. Dinucleotidesensing proteins: linking signaling networks and regulating transcription. Sci. Signal. 1:pe38.
    • (2008) Sci. Signal. , vol.1
    • Lamb, H.K.1    Stammers, D.K.2    Hawkins, A.R.3
  • 21
    • 0023860471 scopus 로고
    • Immunization with nanogram quantities of nitrocellulose-bound antigen, electroblotted from sodium dodecyl sulphate-polyacrylamide gels
    • Larsson, A., and B. O. Nilsson. 1988. Immunization with nanogram quantities of nitrocellulose-bound antigen, electroblotted from sodium dodecyl sulphate-polyacrylamide gels. Scand. J. Immunol. 27:305-309.
    • (1988) Scand. J. Immunol. , vol.27 , pp. 305-309
    • Larsson, A.1    Nilsson, B.O.2
  • 22
    • 0037015160 scopus 로고    scopus 로고
    • Mutational, kinetic, and NMR studies of the mechanism of E. coli GDP-mannose mannosyl hydrolase, an unusual Nudix enzyme
    • Legler, P. M., M. A. Massiah, and A. S. Mildvan. 2002. Mutational, kinetic, and NMR studies of the mechanism of E. coli GDP-mannose mannosyl hydrolase, an unusual Nudix enzyme. Biochemistry 41:10834-10848.
    • (2002) Biochemistry , vol.41 , pp. 10834-10848
    • Legler, P.M.1    Massiah, M.A.2    Mildvan, A.S.3
  • 23
    • 61449241796 scopus 로고    scopus 로고
    • Structure and biological function of the RNA pyrophosphohydrolase BdRppH from Bdellovibrio bacteriovorus
    • Messing, S. A., et al. 2009. Structure and biological function of the RNA pyrophosphohydrolase BdRppH from Bdellovibrio bacteriovorus. Structure 17:472-481.
    • (2009) Structure , vol.17 , pp. 472-481
    • Messing, S.A.1
  • 24
    • 9744224380 scopus 로고    scopus 로고
    • Structures and mechanisms of Nudix hydrolases
    • Mildvan, A. S., et al. 2005. Structures and mechanisms of Nudix hydrolases. Arch. Biochem. Biophys. 433:129-143.
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 129-143
    • Mildvan, A.S.1
  • 25
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M., et al. 1998. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comp. Chem. 19:1639-1662.
    • (1998) J. Comp. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. A 276:307-326.
    • (1997) Macromol. Crystallogr. A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 40049099848 scopus 로고    scopus 로고
    • Mechanism of activation and inhibition of the HER4/ErbB4 kinase
    • Qiu, C., et al. 2008. Mechanism of activation and inhibition of the HER4/ErbB4 kinase. Structure 16:460-467.
    • (2008) Structure , vol.16 , pp. 460-467
    • Qiu, C.1
  • 28
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: the European Molecular Biology Open Software Suite
    • Rice, P., I. Longden, and A. Bleasby. 2000. EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet. 16:276-277.
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 29
    • 41849121949 scopus 로고    scopus 로고
    • Transcriptional regulation of NAD metabolism in bacteria: NrtR family of Nudix-related regulators
    • Rodionov, D. A., et al. 2008. Transcriptional regulation of NAD metabolism in bacteria: NrtR family of Nudix-related regulators. Nucleic Acids Res. 36:2047-2059.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2047-2059
    • Rodionov, D.A.1
  • 30
    • 0014481339 scopus 로고
    • Sporulation and production of antibiotics, exoenzymes, and exotoxins
    • Schaeffer, P. 1969. Sporulation and production of antibiotics, exoenzymes, and exotoxins. Bacteriol. Rev. 33:48-71.
    • (1969) Bacteriol. Rev. , vol.33 , pp. 48-71
    • Schaeffer, P.1
  • 31
    • 38949156197 scopus 로고    scopus 로고
    • Structural basis of dcp2 recognition and activation by dcp1
    • She, M., et al. 2008. Structural basis of dcp2 recognition and activation by dcp1. Mol. Cell 29:337-349.
    • (2008) Mol. Cell , vol.29 , pp. 337-349
    • She, M.1
  • 32
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger, T. C. 2003. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. D Biol. Crystallogr. 59:38-44.
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 33
    • 0037242985 scopus 로고    scopus 로고
    • Automated side-chain model building and sequence assignment by template matching
    • Terwilliger, T. C. 2003. Automated side-chain model building and sequence assignment by template matching. Acta Crystallogr. D Biol. Crystallogr. 59:45-49.
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 45-49
    • Terwilliger, T.C.1
  • 35
    • 0001940082 scopus 로고
    • MAD phasing: treatment of dispersive differences as isomorphous replacement information
    • Terwilliger, T. C. 1994. MAD phasing: treatment of dispersive differences as isomorphous replacement information. Acta Crystallogr. D Biol. Crystallogr. 50:17-23.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 17-23
    • Terwilliger, T.C.1
  • 38
    • 0002016798 scopus 로고
    • Isomorphous replacement: effects of errors on the phase probability-distribution
    • Terwilliger, T. C., and D. Eisenberg. 1987. Isomorphous replacement: effects of errors on the phase probability-distribution. Acta Crystallogr. A 43:6-13.
    • (1987) Acta Crystallogr. A , vol.43 , pp. 6-13
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 39
    • 0001473634 scopus 로고
    • Unbiased 3-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functions
    • Terwilliger, T. C., and D. Eisenberg. 1983. Unbiased 3-dimensional refinement of heavy-atom parameters by correlation of origin-removed Patterson functions. Acta Crystallogr. A 39:813-817.
    • (1983) Acta Crystallogr. A , vol.39 , pp. 813-817
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 40
    • 80055004570 scopus 로고
    • Generalized method of determining heavy-atom positions using the difference Patterson function
    • Terwilliger, T. C., S. H. Kim, and D. Eisenberg. 1987. Generalized method of determining heavy-atom positions using the difference Patterson function. Acta Crystallogr. A 43:1-5.
    • (1987) Acta Crystallogr. A , vol.43 , pp. 1-5
    • Terwilliger, T.C.1    Kim, S.H.2    Eisenberg, D.3
  • 41
    • 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., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 42
    • 0015620349 scopus 로고
    • Technique for ultracryotomy of cell suspensions and tissues
    • Tokuyasu, K. T. 1973. Technique for ultracryotomy of cell suspensions and tissues. J. Cell Biol. 57:551-565.
    • (1973) J. Cell Biol. , vol.57 , pp. 551-565
    • Tokuyasu, K.T.1
  • 43
    • 58149311440 scopus 로고    scopus 로고
    • The crystal structure of human cleavage and polyadenylation specific factor-5 reveals a dimeric Nudix protein with a conserved catalytic site
    • Tresaugues, L., et al. 2008. The crystal structure of human cleavage and polyadenylation specific factor-5 reveals a dimeric Nudix protein with a conserved catalytic site. Proteins 73:1047-1052.
    • (2008) Proteins , vol.73 , pp. 1047-1052
    • Tresaugues, L.1
  • 44
    • 0034477023 scopus 로고    scopus 로고
    • Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core
    • Willis, M. A., B. Bishop, L. Regan, and A. T. Brunger. 2000. Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core. Structure 8:1319-1328.
    • (2000) Structure , vol.8 , pp. 1319-1328
    • Willis, M.A.1    Bishop, B.2    Regan, L.3    Brunger, A.T.4
  • 45
    • 2642579311 scopus 로고    scopus 로고
    • The 26 Nudix hydrolases of Bacillus cereus, a close relative of Bacillus anthracis
    • Xu, W., C. A. Dunn, C. R. Jones, G. D'Souza, and M. J. Bessman. 2004. The 26 Nudix hydrolases of Bacillus cereus, a close relative of Bacillus anthracis. J. Biol. Chem. 279:24861-24865.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24861-24865
    • Xu, W.1    Dunn, C.A.2    Jones, C.R.3    D'Souza, G.4    Bessman, M.J.5
  • 46
    • 0242501006 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose
    • Yagi, T., et al. 2003. Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose. Biochem. J. 370:409-415.
    • (2003) Biochem. J. , vol.370 , pp. 409-415
    • Yagi, T.1
  • 47


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.