메뉴 건너뛰기




Volumn 275, Issue 23, 2008, Pages 5855-5864

Structural and functional studies on a mesophilic stationary phase survival protein (Sur E) from Salmonella typhimurium

Author keywords

Divalent metal ion; Domain swapping; Mononucleotidase; Stationary phase; Sur E

Indexed keywords

4 NITROPHENYL PHOSPHATE; BACTERIAL PROTEIN; MAGNESIUM; METAL ION; PHOSPHATE; SURE PROTEIN; UNCLASSIFIED DRUG;

EID: 55949100453     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06715.x     Document Type: Article
Times cited : (11)

References (25)
  • 1
    • 0028109045 scopus 로고
    • A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome
    • Li C, Ichikawa JK, Ravetto JJ, Kuo HC, Fu JC Clarke S (1994) A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome. J Bacteriol 176, 6015 6022.
    • (1994) J Bacteriol , vol.176 , pp. 6015-6022
    • Li, C.1    Ichikawa, J.K.2    Ravetto, J.J.3    Kuo, H.C.4    Fu, J.C.5    Clarke, S.6
  • 2
    • 0035895278 scopus 로고    scopus 로고
    • Genetic architecture of thermal adaptation in Escherichia coli
    • Riehle MM, Bennett AF Long AD (2001) Genetic architecture of thermal adaptation in Escherichia coli. Proc Natl Acad Sci U S A 98, 525 530.
    • (2001) Proc Natl Acad Sci U S a , vol.98 , pp. 525-530
    • Riehle, M.M.1    Bennett, A.F.2    Long, A.D.3
  • 3
    • 0026649247 scopus 로고
    • Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a genomic sequence from the yeast Yarrowia lipolytica identifies a new phosphatase
    • Treton BY, Le Dall MT Gaillardin CM (1992) Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a genomic sequence from the yeast Yarrowia lipolytica identifies a new phosphatase. Curr Genet 22, 345 355.
    • (1992) Curr Genet , vol.22 , pp. 345-355
    • Treton, B.Y.1    Le Dall, M.T.2    Gaillardin, C.M.3
  • 4
    • 11144227620 scopus 로고    scopus 로고
    • General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG
    • Proudfoot M, Kuznetsova E, Brown G, Rao NN, Kitagawa M, Mori H, Savchenko A Yakunin AF (2004) General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG. J Biol Chem 279, 54687 54694.
    • (2004) J Biol Chem , vol.279 , pp. 54687-54694
    • Proudfoot, M.1    Kuznetsova, E.2    Brown, G.3    Rao, N.N.4    Kitagawa, M.5    Mori, H.6    Savchenko, A.7    Yakunin, A.F.8
  • 5
    • 0032587711 scopus 로고    scopus 로고
    • Inhibition of GTPgammaS-dependent L-isoaspartyl protein methylation by tyrosine kinase inhibitors in kidney
    • Bilodeau D Beliveau R (1999) Inhibition of GTPgammaS-dependent L-isoaspartyl protein methylation by tyrosine kinase inhibitors in kidney. Cell Signal 11, 45 52.
    • (1999) Cell Signal , vol.11 , pp. 45-52
    • Bilodeau, D.1    Beliveau, R.2
  • 6
    • 0032189541 scopus 로고    scopus 로고
    • Mutations in the Escherichia coli surE gene increase isoaspartyl accumulation in a strain lacking the pcm repair methyltransferase but suppress stress-survival phenotypes
    • Visick JE, Ichikawa JK Clarke S (1998) Mutations in the Escherichia coli surE gene increase isoaspartyl accumulation in a strain lacking the pcm repair methyltransferase but suppress stress-survival phenotypes. FEMS Microbiol Lett 167, 19 25.
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 19-25
    • Visick, J.E.1    Ichikawa, J.K.2    Clarke, S.3
  • 7
    • 0001679473 scopus 로고    scopus 로고
    • ALIGN: A program to superinpose protein coordinates accounting for insertions and deletions
    • Cohen GE (1997) ALIGN: a program to superinpose protein coordinates accounting for insertions and deletions. J Appl Cryst 30, 1160 1161.
    • (1997) J Appl Cryst , vol.30 , pp. 1160-1161
    • Cohen, G.E.1
  • 10
    • 34447107887 scopus 로고    scopus 로고
    • Crystal structure of the stationary phase survival protein SurE with metal ion and AMP
    • Iwasaki W Miki K (2007) Crystal structure of the stationary phase survival protein SurE with metal ion and AMP. J Mol Biol 371, 123 136.
    • (2007) J Mol Biol , vol.371 , pp. 123-136
    • Iwasaki, W.1    Miki, K.2
  • 11
    • 0037424607 scopus 로고    scopus 로고
    • Structure and function of an archaeal homolog of survival protein e (SurEalpha): An acid phosphatase with purine nucleotide specificity
    • Mura C, Katz JE, Clarke SG Eisenberg D (2003) Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity. J Mol Biol 326, 1559 1575.
    • (2003) J Mol Biol , vol.326 , pp. 1559-1575
    • Mura, C.1    Katz, J.E.2    Clarke, S.G.3    Eisenberg, D.4
  • 12
    • 0025240438 scopus 로고
    • Protein model structure evaluation using the solvation free energy of folding
    • Chiche L, Gregoret LM, Cohen FE Kollman PA (1990) Protein model structure evaluation using the solvation free energy of folding. Proc Natl Acad Sci USA 87, 3240 3243.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3240-3243
    • Chiche, L.1    Gregoret, L.M.2    Cohen, F.E.3    Kollman, P.A.4
  • 14
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowsky Z 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
    • Otwinowsky, Z.1    Minor, W.2
  • 15
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr A 50, 157 163.
    • (1994) Acta Crystallogr a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 17
  • 18
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value. Methods and applications
    • Brunger AT (1993) Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Crystallogr D 49, 24 36.
    • (1993) Acta Crystallogr D , vol.49 , pp. 24-36
    • Brunger, A.T.1
  • 19
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski RA, Moss DS Thornton JM (1993) Main-chain bond lengths and bond angles in protein structures. J Mol Biol 231, 1049 1067.
    • (1993) J Mol Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 20
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College, London.
    • Hubbard SJ Thornton JM (1993) NACCESS, Computer Program. Department of Biochemistry and Molecular Biology, University College, London.
    • (1993) NACCESS, Computer Program.
    • Hubbard, S.J.1    Thornton, J.M.2
  • 21
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774 797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 22
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L Sander C (1995) Dali: a network tool for protein structure comparison. Trends Biochem Sci 20, 478 480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 23
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins
    • Binkowski TA, Naghibzadeh S Liang J (2003) CASTp: computed atlas of surface topography of proteins. Nucleic Acids Res 31, 3352 3355.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3
  • 25
    • 0037314068 scopus 로고    scopus 로고
    • TopDraw: A sketchpad for protein structure topology cartoons
    • Bond CS (2003) TopDraw: a sketchpad for protein structure topology cartoons. Bioinformatics 19, 311 312.
    • (2003) Bioinformatics , vol.19 , pp. 311-312
    • Bond, C.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.