메뉴 건너뛰기




Volumn 65, Issue 4, 2006, Pages 1032-1035

Crystal structure of the diadenosine tetraphosphate hydrolase from Shigella flexneri 2α

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DIADENOSINE TETRAPHOSPHATE; DIADENOSINE TETRAPHOSPHATE HYDROLASE; HYDROLASE; UNCLASSIFIED DRUG;

EID: 33751085630     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21106     Document Type: Article
Times cited : (7)

References (17)
  • 1
    • 0014007431 scopus 로고
    • Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase
    • Zamecnik PC, Stephenson ML, Janeway CM, Randerath K. Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase. Biochem Biophys Res Commun 1966;24:91-97.
    • (1966) Biochem Biophys Res Commun , vol.24 , pp. 91-97
    • Zamecnik, P.C.1    Stephenson, M.L.2    Janeway, C.M.3    Randerath, K.4
  • 2
    • 0020169938 scopus 로고
    • Mechanism of synthesis of adenosine(5′) tetraphospho (5′)adenosine (AppppA) by aminoacyl-tRNA synthetases
    • Goerlich O, Foeckler R, Holler E. Mechanism of synthesis of adenosine(5′) tetraphospho (5′)adenosine (AppppA) by aminoacyl-tRNA synthetases. Eur J Biochem 1982;126:135-142.
    • (1982) Eur J Biochem , vol.126 , pp. 135-142
    • Goerlich, O.1    Foeckler, R.2    Holler, E.3
  • 3
    • 0032496375 scopus 로고    scopus 로고
    • Diadenosine oligophosphates (ApnA), a novel class of signaling molecules?
    • Kisselev LL, Justesen J, Wolfson AD, Frolova LY. Diadenosine oligophosphates (ApnA), a novel class of signaling molecules? FEBS Lett 1998;427:157-163.
    • (1998) FEBS Lett , vol.427 , pp. 157-163
    • Kisselev, L.L.1    Justesen, J.2    Wolfson, A.D.3    Frolova, L.Y.4
  • 4
    • 0033796736 scopus 로고    scopus 로고
    • Specific and nonspecific enzyme involved in the catabolism of mononucleoside and dinuceoside polyphosphases
    • Guranowski A. Specific and nonspecific enzyme involved in the catabolism of mononucleoside and dinuceoside polyphosphases. Pharmacol Ther 2000;87:117-139.
    • (2000) Pharmacol Ther , vol.87 , pp. 117-139
    • Guranowski, A.1
  • 5
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter CW, Sweet RM, editors. San Diego CA: Academic Press
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter CW, Sweet RM, editors. Methods in enzymology, Vol. 276: Macromolecular crystallography, part A. San Diego CA: Academic Press; 1997. pp 307-326.
    • (1997) Methods in Enzymology, Vol. 276: Macromolecular Crystallography, Part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 6
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson WA. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 1991;254:51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 9
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 10
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D Biol Crystallogr 1997;53:240-255.
    • (1997) Acta Cryst D Biol Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 11
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4
    • Collaborative Computational Project 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 12
    • 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 JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 13
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999;15:305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 15
    • 0030765455 scopus 로고    scopus 로고
    • Dali/FSSP classification of three-dimensional protein folds
    • Holm L, Sander C. Dali/FSSP classification of three-dimensional protein folds. Nucleic Acids Res 1997;25:231-234.
    • (1997) Nucleic Acids Res , vol.25 , pp. 231-234
    • Holm, L.1    Sander, C.2
  • 16
    • 0028053053 scopus 로고
    • Conservation analysis and structure prediction of the protein serine/threonine phosphatases. Sequence similarity with diadenosine tetraphosphatase from Escherichia coli suggests homology to the protein phosphatases
    • Barton GJ, Cohen PT, Barford D. Conservation analysis and structure prediction of the protein serine/threonine phosphatases. Sequence similarity with diadenosine tetraphosphatase from Escherichia coli suggests homology to the protein phosphatases. Eur J Biochem 1994;220:225-237.
    • (1994) Eur J Biochem , vol.220 , pp. 225-237
    • Barton, G.J.1    Cohen, P.T.2    Barford, D.3
  • 17
    • 0034687659 scopus 로고    scopus 로고
    • Structure of the bacteriophage λ Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes
    • Voegtli WC, White DJ, Reiter NJ, Rusnak F, Rosenzweig AC. Structure of the bacteriophage λ Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes. Biochemistry 2000;39:15365-15374.
    • (2000) Biochemistry , vol.39 , pp. 15365-15374
    • Voegtli, W.C.1    White, D.J.2    Reiter, N.J.3    Rusnak, F.4    Rosenzweig, A.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.