메뉴 건너뛰기




Volumn 11, Issue 8, 2003, Pages 1015-1023

Structure and mechanism of MT-ADPRase, a Nudix hydrolase from Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GADOLINIUM; HYDROLASE; MAGNESIUM ION; MANGANESE; METAL ION; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN SUBUNIT;

EID: 0043133626     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(03)00154-0     Document Type: Article
Times cited : (56)

References (26)
  • 1
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes
    • Bessman M.J., Frick D.N., O'Handley S.F. The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. J. Biol. Chem. 271:1996;25059-25062.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 2
    • 0030767713 scopus 로고    scopus 로고
    • Free R value: Cross-validation in crystallography
    • Brunger A.T. Free R value. cross-validation in crystallography Methods Enzymol. 277:1997;366-396.
    • (1997) Methods Enzymol. , vol.277 , pp. 366-396
    • Brunger, A.T.1
  • 5
    • 0033527537 scopus 로고    scopus 로고
    • Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance
    • Dunn C.A., O'Handley S.F., Frick D.N., Bessman M.J. Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance. J. Biol. Chem. 274:1999;32318-32324.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32318-32324
    • Dunn, C.A.1    O'Handley, S.F.2    Frick, D.N.3    Bessman, M.J.4
  • 6
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to Molscript version 1.4, including reading and countouring of electron density maps
    • Esnouf R.M. Further additions to Molscript version 1.4, including reading and countouring of electron density maps. Acta Crystallogr. D. 55:1999;938-940.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 7
    • 0039105798 scopus 로고    scopus 로고
    • Specific ADP-ribose pyrophosphatase from Artemia cysts and rat liver: Effects of nitroprusside, fluoride and ionic strength
    • Fernandez A., Ribeiro J.M., Costas M.J., Pinto R.M., Canales J., Cameselle J.C. Specific ADP-ribose pyrophosphatase from Artemia cysts and rat liver. effects of nitroprusside, fluoride and ionic strength Biochim. Biophys. Acta. 1290:1996;121-127.
    • (1996) Biochim. Biophys. Acta , vol.1290 , pp. 121-127
    • Fernandez, A.1    Ribeiro, J.M.2    Costas, M.J.3    Pinto, R.M.4    Canales, J.5    Cameselle, J.C.6
  • 8
    • 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., Bianchet M.A., Bessman M.J., Amzel L.M. The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family. Nat. Struct. Biol. 8:2001;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
  • 10
    • 84889120137 scopus 로고
    • Improved methods for binding protein models to electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjelgaard M. Improved methods for binding protein models to electron density maps and the location of errors in these models. Acta Crystallogr. A. 42:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.42 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 11
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • Jones T.A., Kjeldgaard M. Electron-density map interpretation. Methods Enzymol. 277:1997;173-208.
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.A.1    Kjeldgaard, M.2
  • 13
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structure
    • Kraulis J. Molscript. a program to produce both detailed and schematic plots of protein structure J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, J.1
  • 14
    • 0000243829 scopus 로고
    • Procheck: A program to check the sterochemical quality of protein structures
    • Laskowski R., MacArthur M., Moss D., Thornton J. Procheck. a program to check the sterochemical quality of protein structures J. Appl. Crystallogr. 26:1993;283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 15
    • 0035102449 scopus 로고    scopus 로고
    • Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics
    • Makarova K.S., Aravind L., Wolf Y.I., Tatusov R.L., Minton K.W., Koonin E.V., Daly M.J. Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics. Microbiol. Mol. Biol. Rev. 65:2001;44-79.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 44-79
    • Makarova, K.S.1    Aravind, L.2    Wolf, Y.I.3    Tatusov, R.L.4    Minton, K.W.5    Koonin, E.V.6    Daly, M.J.7
  • 17
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merrit E., Bacon D. Raster3D. photorealistic molecular graphics Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.1    Bacon, D.2
  • 18
    • 0032488819 scopus 로고    scopus 로고
    • Orf186 represents a new member of the Nudix hydrolases, active on adenosine(5′)triphospho(5′)adenosine, ADP-ribose, and NADH
    • O'Handley S.F., Frick D.N., Dunn C.A., Bessman M.J. Orf186 represents a new member of the Nudix hydrolases, active on adenosine(5′)triphospho(5′)adenosine, ADP-ribose, and NADH. J. Biol. Chem. 273:1998;3192-3197.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3192-3197
    • O'Handley, S.F.1    Frick, D.N.2    Dunn, C.A.3    Bessman, M.J.4
  • 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. 277:1997;307-326.
    • (1997) Methods Enzymol. , vol.277 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0034792227 scopus 로고    scopus 로고
    • Changes in gene expression in macrophages infected with Mycobacterium tuberculosis: A combined transcriptomic and proteomic approach
    • Ragno S., Romano M., Howell S., Pappin D.J., Jenner P.J., Colston M.J. Changes in gene expression in macrophages infected with Mycobacterium tuberculosis. a combined transcriptomic and proteomic approach Immunology. 104:2001;99-108.
    • (2001) Immunology , vol.104 , pp. 99-108
    • Ragno, S.1    Romano, M.2    Howell, S.3    Pappin, D.J.4    Jenner, P.J.5    Colston, M.J.6
  • 22
    • 0032618538 scopus 로고    scopus 로고
    • ADP-ribose pyrophosphatase-I partially purified from livers of rats overdosed with acetaminophen reveals enzyme inhibition in vivo reverted in vitro by dithiothreitol
    • Ribeiro J.M., Costas M.J., Cameselle J.C. ADP-ribose pyrophosphatase-I partially purified from livers of rats overdosed with acetaminophen reveals enzyme inhibition in vivo reverted in vitro by dithiothreitol. J. Biochem. Mol. Toxicol. 13:1999;171-177.
    • (1999) J. Biochem. Mol. Toxicol. , vol.13 , pp. 171-177
    • Ribeiro, J.M.1    Costas, M.J.2    Cameselle, J.C.3
  • 23
    • 0035799396 scopus 로고    scopus 로고
    • Human placenta hydrolases active on free ADP-ribose: An ADP-sugar pyrophosphatase and a specific ADP-ribose pyrophosphatase
    • Ribeiro J.M., Carloto A., Costas M.J., Cameselle J.C. Human placenta hydrolases active on free ADP-ribose. an ADP-sugar pyrophosphatase and a specific ADP-ribose pyrophosphatase Biochim. Biophys. Acta. 1526:2001;86-94.
    • (2001) Biochim. Biophys. Acta , vol.1526 , pp. 86-94
    • Ribeiro, J.M.1    Carloto, A.2    Costas, M.J.3    Cameselle, J.C.4
  • 24
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for Mir and Mad
    • Terwilliger T.C., Berendzen J. Automated structure solution for Mir and Mad. Acta Crystallogr. D. 55:1999;849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.