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Volumn 326, Issue 5, 2003, Pages 1559-1575

Structure and function of an archaeal homolog of survival protein E (SurEα): An acid phosphatase with purine nucleotide specificity

Author keywords

Acid phosphatase; Archaeal protein; Domain swapping; Rossmann like fold; Survival protein E

Indexed keywords

ACID PHOSPHATASE; ARCHAEAL PROTEIN; GUANOSINE PHOSPHATE; PURINE NUCLEOTIDE; SURVIVAL PROTEIN E; UNCLASSIFIED DRUG;

EID: 0037424607     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00056-1     Document Type: Article
Times cited : (25)

References (35)
  • 1
    • 0028109045 scopus 로고
    • A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome
    • Li C., Ichikawa J.K., Ravetto J.J., Kuo H.C., Fu J.C., Clarke S. A new gene involved in stationary-phase survival located at 59 minutes on the Escherichia coli chromosome. J. Bacteriol. 176:1994;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
    • 0030696850 scopus 로고    scopus 로고
    • Growth-phase-dependent transcriptional regulation of the pcm and surE genes required for stationary-phase survival of Escherichia coli
    • Li C., Wu P.Y., Hsieh M. Growth-phase-dependent transcriptional regulation of the pcm and surE genes required for stationary-phase survival of Escherichia coli. Microbiology. 143:1997;3513-3520.
    • (1997) Microbiology , vol.143 , pp. 3513-3520
    • Li, C.1    Wu, P.Y.2    Hsieh, M.3
  • 3
    • 0028019587 scopus 로고
    • The role of the sigma factor sigma S (KatF) in bacterial global regulation
    • Loewen P.C., Hengge-Aronis R. The role of the sigma factor sigma S (KatF) in bacterial global regulation. Annu. Rev. Microbiol. 48:1994;53-80.
    • (1994) Annu. Rev. Microbiol , vol.48 , pp. 53-80
    • Loewen, P.C.1    Hengge-Aronis, R.2
  • 4
    • 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 J.E., Ichikawa J.K., Clarke S. 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. Letters. 167:1998;19-25.
    • (1998) FEMS Microbiol. Letters , vol.167 , pp. 19-25
    • Visick, J.E.1    Ichikawa, J.K.2    Clarke, S.3
  • 5
    • 0035895278 scopus 로고    scopus 로고
    • Genetic architecture of thermal adaptation in Escherichia coli
    • Riehle M.M., Bennett A.F., Long A.D. Genetic architecture of thermal adaptation in Escherichia coli. Proc. Natl Acad. Sci. USA. 98:2001;525-530.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 525-530
    • Riehle, M.M.1    Bennett, A.F.2    Long, A.D.3
  • 6
    • 0026649247 scopus 로고
    • Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a genomic sequence from the yeast Yarrowia lipolytica identifies a new phosphatase
    • Treton B.Y., Le Dall M.T., Gaillardin C.M. Complementation of Saccharomyces cerevisiae acid phosphatase mutation by a genomic sequence from the yeast Yarrowia lipolytica identifies a new phosphatase. Curr. Genet. 22:1992;345-355.
    • (1992) Curr. Genet. , vol.22 , pp. 345-355
    • Treton, B.Y.1    Le Dall, M.T.2    Gaillardin, C.M.3
  • 7
    • 0034870623 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family
    • Lee J.Y., Kwak J.E., Moon J., Eom S.H., Liong E.C., Pedelacq J.D., et al. Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family. Nature Struct. Biol. 8:2001;789-794.
    • (2001) Nature Struct. Biol. , vol.8 , pp. 789-794
    • Lee, J.Y.1    Kwak, J.E.2    Moon, J.3    Eom, S.H.4    Liong, E.C.5    Pedelacq, J.D.6
  • 8
    • 0035190121 scopus 로고    scopus 로고
    • Structure of Thermotoga maritima stationary phase survival protein SurE: A novel acid phosphatase
    • Zhang R.G., Skarina T., Katz J.E., Beasley S., Khachatryan A., Vyas S., et al. Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase. Structure (Camb). 9:2001;1095-1106.
    • (2001) Structure (Camb) , vol.9 , pp. 1095-1106
    • Zhang, R.G.1    Skarina, T.2    Katz, J.E.3    Beasley, S.4    Khachatryan, A.5    Vyas, S.6
  • 10
    • 0034084540 scopus 로고    scopus 로고
    • Objective comparison of protein structures: Error-scaled difference distance matrices
    • Schneider T.R. Objective comparison of protein structures: error-scaled difference distance matrices. Acta Crystallog. sect. D. 56:2000;714-721.
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 714-721
    • Schneider, T.R.1
  • 11
    • 0036008503 scopus 로고    scopus 로고
    • A genetic algorithm for the identification of conformationally invariant regions in protein molecules
    • Schneider T.R. A genetic algorithm for the identification of conformationally invariant regions in protein molecules. Acta Crystallog. sect. D. 58:2002;195-208.
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 195-208
    • Schneider, T.R.1
  • 12
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • Colovos C., Yeates T.O. Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci. 2:1993;1511-1519.
    • (1993) Protein Sci. , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 14
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • Eisenberg D., Luthy R., Bowie J.U. VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol. 277:1997;396-406.
    • (1997) Methods Enzymol. , vol.277 , pp. 396-406
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 15
    • 0034044449 scopus 로고    scopus 로고
    • Phosphorylation of tubulin tyrosine ligase: A potential mechanism for regulation of alpha-tubulin tyrosination
    • Idriss H.T. Phosphorylation of tubulin tyrosine ligase: a potential mechanism for regulation of alpha-tubulin tyrosination. Cell Motil. Cytoskeleton. 46:2000;1-5.
    • (2000) Cell Motil. Cytoskeleton , vol.46 , pp. 1-5
    • Idriss, H.T.1
  • 16
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger M.P., Bennett M.J., Eisenberg D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Advan. Protein Chem. 50:1997;61-122.
    • (1997) Advan. Protein Chem. , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 17
    • 0035190116 scopus 로고    scopus 로고
    • Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus
    • O'Neill J.W., Kim D.E., Johnsen K., Baker D., Zhang K.Y. Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus. Structure. 9:2001;1017-1027.
    • (2001) Structure , vol.9 , pp. 1017-1027
    • O'Neill, J.W.1    Kim, D.E.2    Johnsen, K.3    Baker, D.4    Zhang, K.Y.5
  • 18
  • 19
  • 20
    • 12644251992 scopus 로고    scopus 로고
    • Response surface methods for optimizing and improving reproducibility of crystal growth
    • Carter C.W. Jr. Response surface methods for optimizing and improving reproducibility of crystal growth. Methods Enzymol. 276A:1997;74-99.
    • (1997) Methods Enzymol. , vol.276 A , pp. 74-99
    • Carter C.W., Jr.1
  • 21
    • 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. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 0030841590 scopus 로고    scopus 로고
    • Collaborative computational project number 4: Providing programs for protein crystallography
    • Dodson E.J., Winn M., Ralph A. Collaborative computational project number 4: providing programs for protein crystallography. Methods Enzymol. 276:1997;620-633.
    • (1997) Methods Enzymol. , vol.276 , pp. 620-633
    • Dodson, E.J.1    Winn, M.2    Ralph, A.3
  • 23
    • 0032128419 scopus 로고    scopus 로고
    • Miscellaneous algorithms for density modification
    • Cowtan K., Main P. Miscellaneous algorithms for density modification. Acta Crystallog. sect. D. 54:1998;487-493.
    • (1998) Acta Crystallog. sect. D , vol.54 , pp. 487-493
    • Cowtan, K.1    Main, P.2
  • 24
    • 0034929414 scopus 로고    scopus 로고
    • A new software routine that automates the fitting of protein X-ray crystallographic electron-density maps
    • Levitt D.G. A new software routine that automates the fitting of protein X-ray crystallographic electron-density maps. Acta Crystallog. sect. D. 57:2001;1013-1019.
    • (2001) Acta Crystallog. sect. D , vol.57 , pp. 1013-1019
    • Levitt, D.G.1
  • 25
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nature Struct. Biol. 6:1999;458-463.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 26
    • 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., Kjeldgaard. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 30
    • 0033990063 scopus 로고    scopus 로고
    • GCG: The Wisconsin Package of sequence analysis programs
    • Womble D.D. GCG: The Wisconsin Package of sequence analysis programs. Methods Mol. Biol. 132:2000;3-22.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 3-22
    • Womble, D.D.1
  • 31
    • 0028177080 scopus 로고
    • A simulation comparison of phylogeny algorithms under equal and unequal evolutionary rates
    • Kuhner M.K., Felsenstein J. A simulation comparison of phylogeny algorithms under equal and unequal evolutionary rates. Mol. Biol. Evol. 11:1994;459-468.
    • (1994) Mol. Biol. Evol. , vol.11 , pp. 459-468
    • Kuhner, M.K.1    Felsenstein, J.2
  • 32
    • 0023053742 scopus 로고
    • Phosphocholine binding immunoglobulin Fab McPC603: An X-ray diffraction study at 2.7 Å
    • Satow Y., Cohen G.H., Padlan E.A., Davies D.R. Phosphocholine binding immunoglobulin Fab McPC603: an X-ray diffraction study at 2.7 Å J. Mol. Biol. 190:1986;593-604. http://www.doe-mbi.ucla.edu/People/Software/ALIGN.html.
    • (1986) J. Mol. Biol. , vol.190 , pp. 593-604
    • Satow, Y.1    Cohen, G.H.2    Padlan, E.A.3    Davies, D.R.4
  • 33
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11:1998;739-747.
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 34
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 35
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:1971;379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2


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