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Volumn 14, Issue 5, 2005, Pages 1350-1356

Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase family

Author keywords

Esterase; Lipase; OVCA2; Serine hydrolase; Yhr049w FSH1; Ymr222c FSH2; Yor280c FSH3

Indexed keywords

ASPARTIC ACID; ESTERASE; HISTIDINE; SERINE; SERINE DEHYDRATASE;

EID: 17744381165     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.051415905     Document Type: Article
Times cited : (21)

References (35)
  • 2
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne, G., Vonrhein, C., Flensburg, C., Schiltz, M., and Paciorek, W. 2003. Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0. Acta Crystallogr. D Biol. Crystallogr. 59: 2023-2030.
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 5
    • 0029161231 scopus 로고
    • The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate
    • Egloff, M.P., Marguet, F., Buono, G., Verger, R., Cambillau, C., and van Tilbeurgh, H. 1995. The 2.46 Å resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Biochemistry 34: 2751-2762.
    • (1995) Biochemistry , vol.34 , pp. 2751-2762
    • Egloff, M.P.1    Marguet, F.2    Buono, G.3    Verger, R.4    Cambillau, C.5    Van Tilbeurgh, H.6
  • 6
    • 0032843737 scopus 로고    scopus 로고
    • Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily
    • Fetrow, J.S., Siew, N., and Skolnick, J. 1999. Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily. FASEB J. 13: 1866-1874.
    • (1999) FASEB J. , vol.13 , pp. 1866-1874
    • Fetrow, J.S.1    Siew, N.2    Skolnick, J.3
  • 7
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D.I., and Metoz, F. 1999. ESPript: Analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 11
    • 0033737598 scopus 로고    scopus 로고
    • High frequency allelic loss on chromosome 17p13.3-p11.1 in esophageal squamous cell carcinomas from a high incidence area in northern China
    • Huang, J., Hu, N., Goldstein, A.M., Emmert-Buck, M.R., Tang, Z.Z., Roth, M.J., Wang, Q.H., Dawsey, S.M., Han, X.Y., Ding, T., et al. 2000. High frequency allelic loss on chromosome 17p13.3-p11.1 in esophageal squamous cell carcinomas from a high incidence area in northern China. Carcinogenesis 21: 2019-2026.
    • (2000) Carcinogenesis , vol.21 , pp. 2019-2026
    • Huang, J.1    Hu, N.2    Goldstein, A.M.3    Emmert-Buck, M.R.4    Tang, Z.Z.5    Roth, M.J.6    Wang, Q.H.7    Dawsey, S.M.8    Han, X.Y.9    Ding, T.10
  • 12
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. 1993. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26: 795-800.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 13
    • 0001603385 scopus 로고    scopus 로고
    • Crystal structure of carboxylesterase from Pseudomonas fluorescens, an α/β hydrolase with broad substrate specificity
    • Kim, K.K., Song, H.K., Shin, D.H., Hwang, K.Y., Choe, S., Yoo, O.J., and Suh, S.W. 1997. Crystal structure of carboxylesterase from Pseudomonas fluorescens, an α/β hydrolase with broad substrate specificity. Structure 5: 1571-1584.
    • (1997) Structure , vol.5 , pp. 1571-1584
    • Kim, K.K.1    Song, H.K.2    Shin, D.H.3    Hwang, K.Y.4    Choe, S.5    Yoo, O.J.6    Suh, S.W.7
  • 15
    • 4544232470 scopus 로고    scopus 로고
    • Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities
    • Liger, D., Graille, M., Zhou, C.Z., Leulliot, N., Quevillon-Cheruel, S., Blondeau, K., Janin, J., and van Tilbeurgh, H. 2004. Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities. J. Biol. Chem. 279: 34890-34897.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34890-34897
    • Liger, D.1    Graille, M.2    Zhou, C.Z.3    Leulliot, N.4    Quevillon-Cheruel, S.5    Blondeau, K.6    Janin, J.7    Van Tilbeurgh, H.8
  • 16
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent
    • Martinez, C., De Geus, P., Lauwereys, M., Matthyssens, G., and Cambillau, C. 1992. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356: 615-618.
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    De Geus, P.2    Lauwereys, M.3    Matthyssens, G.4    Cambillau, C.5
  • 17
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G., Vagin, A., and Dodson, E. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53: 240-255.
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.1    Vagin, A.2    Dodson, E.3
  • 18
    • 0032784276 scopus 로고    scopus 로고
    • α/β Hydrolase fold enzymes: The family keeps growing
    • Nardini, M. and Dijkstra, B.W. 1999. α/β Hydrolase fold enzymes: The family keeps growing. Curr. Opin. Struct. Biol. 9: 732-737.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 19
    • 0026540411 scopus 로고
    • The α/β hydrolase fold
    • Ollis, D.L. and Goldman, A. 1992. The α/β hydrolase fold. Protein Eng. 5: 197-211.
    • (1992) Protein Eng. , vol.5 , pp. 197-211
    • Ollis, D.L.1    Goldman, A.2
  • 21
    • 0345864027 scopus 로고    scopus 로고
    • The Catalytic Site Atlas: A resource of catalytic sites and residues identified in enzymes using structural data
    • Porter, C.T., Bartlett, G.J., and Thornton, J.M. 2004. The Catalytic Site Atlas: A resource of catalytic sites and residues identified in enzymes using structural data. Nucleic Acids Res. 32: D129-D133.
    • (2004) Nucleic Acids Res. , vol.32
    • Porter, C.T.1    Bartlett, G.J.2    Thornton, J.M.3
  • 28
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution and density modification
    • Terwilliger, T.C. 2003. SOLVE and RESOLVE: Automated structure solution and density modification. Methods Enzymol. 374: 22-37.
    • (2003) Methods Enzymol. , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 29
    • 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., Higgins, D.G., and Gibson, T.J. 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
  • 30
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • Vagin, A.A. and Isupov, M.N. 2001. Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps. Acta Crystallogr. D Biol. Crystallogr. 57: 1451-1456.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 1451-1456
    • Vagin, A.A.1    Isupov, M.N.2
  • 31
    • 0035946913 scopus 로고    scopus 로고
    • The crystal structure of Bacillus subtilis lipase: A minimal α/β hydrolase fold enzyme
    • van Pouderoyen, G., Eggert, T., Jaeger, K.E., and Dijkstra, B.W. 2001. The crystal structure of Bacillus subtilis lipase: A minimal α/β hydrolase fold enzyme. J. Mol. Biol. 309: 215-226.
    • (2001) J. Mol. Biol. , vol.309 , pp. 215-226
    • Van Pouderoyen, G.1    Eggert, T.2    Jaeger, K.E.3    Dijkstra, B.W.4
  • 34
    • 0032431024 scopus 로고    scopus 로고
    • Structure-based assignment of the biochemical function of a hypothetical protein: A test case of structural genomics
    • Zarembinski, T.I., Hung, L.W., Mueller-Dieckmann, H.J., Kim, K.K., Yokota, H., Kim, R., and Kim, S.H. 1998. Structure-based assignment of the biochemical function of a hypothetical protein: A test case of structural genomics. Proc. Natl. Acad. Sci. 95: 15189-15193.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 15189-15193
    • Zarembinski, T.I.1    Hung, L.W.2    Mueller-Dieckmann, H.J.3    Kim, K.K.4    Yokota, H.5    Kim, R.6    Kim, S.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.