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Volumn 188, Issue 15, 2006, Pages 5606-5617

Crystal structure of TDP-fucosamine acetyltransferase (WecD) from Escherichia coli, an enzyme required for enterobacterial common antigen synthesis

Author keywords

[No Author keywords available]

Indexed keywords

4 ACETAMIDO 4,6 DIDEOXY DEXTRO GALACTOSE; ACETYL COENZYME A; ACYLTRANSFERASE; AMINOGLYCOSIDE ANTIBIOTIC AGENT; BACTERIAL ANTIGEN; BILE SALT; CARBOXYLIC ACID; COENZYME A; ENTEROBACTERIAL COMMON ANTIGEN; HISTONE; N ACETYL DEXTRO MANNOSAMINURONIC ACID; N ACETYLGLUCOSAMINE; POLYSACCHARIDE; PROTEIN WECD; SEROTONIN; TRISACCHARIDE; TYROSINE; UNCLASSIFIED DRUG;

EID: 33746591760     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00306-06     Document Type: Article
Times cited : (26)

References (80)
  • 1
    • 0345826027 scopus 로고    scopus 로고
    • High resolution X-ray structure of dTDP-glucose-4,6-dehydratase from Streptomyces venezuelae
    • Allard, S. T., W. W. Cleland, and H. M. Holden. 2004. High resolution X-ray structure of dTDP-glucose-4,6-dehydratase from Streptomyces venezuelae. J. Biol. Chem. 279:2211-2220.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2211-2220
    • Allard, S.T.1    Cleland, W.W.2    Holden, H.M.3
  • 2
    • 0033579559 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase Hpa2: A tetrameric member of the Gcn5-related N-acetyltransferase superfamily family
    • Angus-Hill, M. L., R. N. Dutnall, S. T. Tafrov, R. Sternglanz, and V. Ramakrishnan. 1999. Crystal structure of the histone acetyltransferase Hpa2: a tetrameric member of the Gcn5-related N-acetyltransferase superfamily family. J. Mol. Biol. 294:1311-1325.
    • (1999) J. Mol. Biol. , vol.294 , pp. 1311-1325
    • Angus-Hill, M.L.1    Dutnall, R.N.2    Tafrov, S.T.3    Sternglanz, R.4    Ramakrishnan, V.5
  • 3
    • 0023664478 scopus 로고
    • Biosynthesis of enterobacterial common antigen in Escherichia coli. In vitro synthesis of lipid-linked intermediates
    • Barr, K., and P. D. Rick. 1987. Biosynthesis of enterobacterial common antigen in Escherichia coli. In vitro synthesis of lipid-linked intermediates. J. Biol. Chem. 262:7142-7150.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7142-7150
    • Barr, K.1    Rick, P.D.2
  • 5
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: The RESP model
    • Bayly, C. I., P. Cieplak, W. D. Cornell, and P. A. Kollman. 1993. A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model. J. Phys. Chem. 97:10269-10280.
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 6
    • 1242283845 scopus 로고    scopus 로고
    • Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNac-pentapeptide: Insights into FemABX family substrates recognition
    • Biarrotte-Sorin, S., A. P. Maillard, J. Delettré, W. Sougakoff, M. Arthur, and C. Mayer. 2004. Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNac-pentapeptide: insights into FemABX family substrates recognition. Structure 12:257-267.
    • (2004) Structure , vol.12 , pp. 257-267
    • Biarrotte-Sorin, S.1    Maillard, A.P.2    Delettré, J.3    Sougakoff, W.4    Arthur, M.5    Mayer, C.6
  • 10
    • 0034637544 scopus 로고    scopus 로고
    • Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP
    • Christendat, D., V. Saridakis, A. Dharamsi, A. Bochkarev, E. F. Pai, C. H. Arrowsmith, and A. M. Edwards. 2000. Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP. J. Biol. Chem. 275:24608-24612.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24608-24612
    • Christendat, D.1    Saridakis, V.2    Dharamsi, A.3    Bochkarev, A.4    Pai, E.F.5    Arrowsmith, C.H.6    Edwards, A.M.7
  • 11
    • 0033168714 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme a
    • Clements, A., J. R. Rojas, R. C. Trievel, L. Wang, S. L. Berger, and R. Marmorstein. 1999. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. EMBO J. 18:3521-3532.
    • (1999) EMBO J. , vol.18 , pp. 3521-3532
    • Clements, A.1    Rojas, J.R.2    Trievel, R.C.3    Wang, L.4    Berger, S.L.5    Marmorstein, R.6
  • 12
    • 0029848559 scopus 로고    scopus 로고
    • Structure and critical residues at the active site of spermidine/spermine-N1-acetyltransferase
    • Coleman, C. S., H. Huang, and A. E. Pegg. 1996. Structure and critical residues at the active site of spermidine/spermine-N1-acetyltransferase. Biochem. J. 316:697-701.
    • (1996) Biochem. J. , vol.316 , pp. 697-701
    • Coleman, C.S.1    Huang, H.2    Pegg, A.E.3
  • 14
    • 0000667030 scopus 로고
    • Application of RESP charges to calculate conformational energies, hydrogen bond energies, and free energies of solvation
    • Cornell, W. D., P. Cieplak, C. I. Bayly, and P. A. Kollman. 1993. Application of RESP charges to calculate conformational energies, hydrogen bond energies, and free energies of solvation. J. Am. Chem. Soc. 115:9620-9631.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9620-9631
    • Cornell, W.D.1    Cieplak, P.2    Bayly, C.I.3    Kollman, P.A.4
  • 15
    • 0031765192 scopus 로고    scopus 로고
    • Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli
    • Danese, P. N., G. R. Oliver, K. Barr, G. D. Bowman, P. D. Rick, and T. J. Silhavy. 1998. Accumulation of the enterobacterial common antigen lipid II biosynthetic intermediate stimulates degP transcription in Escherichia coli. J. Bacteriol. 180:5875-5884.
    • (1998) J. Bacteriol. , vol.180 , pp. 5875-5884
    • Danese, P.N.1    Oliver, G.R.2    Barr, K.3    Bowman, G.D.4    Rick, P.D.5    Silhavy, T.J.6
  • 16
    • 0026754531 scopus 로고
    • Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes
    • Daniels, D. L., G. Plunkett III, V. Burland, and F. R. Blattner. 1992. Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. Science 257:771-778.
    • (1992) Science , vol.257 , pp. 771-778
    • Daniels, D.L.1    Plunkett III, G.2    Burland, V.3    Blattner, F.R.4
  • 17
    • 0032579377 scopus 로고    scopus 로고
    • Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (E.G. 2.3.1.87)
    • De Angelis, J., J. Gastel, D. C. Klein, and P. A. Cole. 1998. Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (E.G. 2.3.1.87). J. Biol. Chem. 273:3045-3050.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3045-3050
    • De Angelis, J.1    Gastel, J.2    Klein, D.C.3    Cole, P.A.4
  • 19
    • 0037334849 scopus 로고    scopus 로고
    • Identification and biosynthesis of cyclic enterobacterial common antigen in Escherichia coli
    • Erbel, P. J., K. Barr, N. Gao, G. J. Gerwig, P. D. Rick, and K. H. Gardner. 2003. Identification and biosynthesis of cyclic enterobacterial common antigen in Escherichia coli. J. Bacteriol. 185:1995-2004.
    • (2003) J. Bacteriol. , vol.185 , pp. 1995-2004
    • Erbel, P.J.1    Barr, K.2    Gao, N.3    Gerwig, G.J.4    Rick, P.D.5    Gardner, K.H.6
  • 20
    • 0035967517 scopus 로고    scopus 로고
    • Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis
    • Farazi, T. A., G. Waksman, and J. I. Gordon. 2001. Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis. Biochemistry 40:6335-6343.
    • (2001) Biochemistry , vol.40 , pp. 6335-6343
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 22
    • 0344837328 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis thymidylate kinase: Structural studies of intermediates along the reaction pathway
    • Fioravanti, E., A. Haouz, T. Ursby, H. Munier-Lehmann, M. Delarue, and D. Bourgeois. 2003. Mycobacterium tuberculosis thymidylate kinase: structural studies of intermediates along the reaction pathway. J. Mol. Biol. 327:1077-1092.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1077-1092
    • Fioravanti, E.1    Haouz, A.2    Ursby, T.3    Munier-Lehmann, H.4    Delarue, M.5    Bourgeois, D.6
  • 23
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet, P., X. Robert, and E. Courcelle. 2003. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31:3320-3323.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 24
    • 0037474532 scopus 로고    scopus 로고
    • Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme a reveals the mechanism for β-lactam aceylation
    • He, H., Y. Ding, M. Bartlam, F. Sun, Y. Le, X. Qin, H. Tang, R. Zhang, A. Joachimiak, J. Liu, N. Zhao, and Z. Rao. 2003. Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for β-lactam aceylation. J. Mol. Biol. 325:1019-1030.
    • (2003) J. Mol. Biol. , vol.325 , pp. 1019-1030
    • He, H.1    Ding, Y.2    Bartlam, M.3    Sun, F.4    Le, Y.5    Qin, X.6    Tang, H.7    Zhang, R.8    Joachimiak, A.9    Liu, J.10    Zhao, N.11    Rao, Z.12
  • 25
    • 0033617457 scopus 로고    scopus 로고
    • The structural basis of ordered substrate binding by serotonin N-acetyltransferase: Enzyme complex at 1.8 Å resolution with a bisubstrate analog
    • Hickman, A. B., M. A. A. Namboodiri, D. C. Klein, and F. Dyda. 1999. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 Å resolution with a bisubstrate analog. Cell 97:361-389.
    • (1999) Cell , vol.97 , pp. 361-389
    • Hickman, A.B.1    Namboodiri, M.A.A.2    Klein, D.C.3    Dyda, F.4
  • 26
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and C. Sander. 1993. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 27
    • 3342987492 scopus 로고    scopus 로고
    • Characterization and investigation of substrate specificity of the sugar aminotransferase WecE from E. coli K12
    • Hwang, B. Y., H. J. Lee, Y. H. Yang, H. S. Joo, and B. G. Kim. 2004. Characterization and investigation of substrate specificity of the sugar aminotransferase WecE from E. coli K12. Chem. Biol. 11:915-925.
    • (2004) Chem. Biol. , vol.11 , pp. 915-925
    • Hwang, B.Y.1    Lee, H.J.2    Yang, Y.H.3    Joo, H.S.4    Kim, B.G.5
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J.-Y. Zou, S. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47:100-119.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 100-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 29
    • 0018193868 scopus 로고
    • Structural studies on the immunogenic form of the enterobacterial common antigen
    • Kiss, P., J. Rinno, G. Schmidt, and H. Mayer. 1978. Structural studies on the immunogenic form of the enterobacterial common antigen. Eur. J. Biochem. 88:211-218.
    • (1978) Eur. J. Biochem. , vol.88 , pp. 211-218
    • Kiss, P.1    Rinno, J.2    Schmidt, G.3    Mayer, H.4
  • 32
    • 0023430366 scopus 로고
    • Monte Carlo-minimization approach to the multiple-minima problem in protein folding
    • Li, Z., and H. A. Scheraga. 1987. Monte Carlo-minimization approach to the multiple-minima problem in protein folding. Proc. Natl. Acad. Sci. USA 84:6611-6615.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6611-6615
    • Li, Z.1    Scheraga, H.A.2
  • 33
    • 0034918673 scopus 로고    scopus 로고
    • Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data
    • Lin, L. Y., T. Sulea, R. Szittner, V. Vassilyev, E. O. Purisima, and E. A. Meighen. 2001. Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data. Prot. Sci. 10:1563-1571.
    • (2001) Prot. Sci. , vol.10 , pp. 1563-1571
    • Lin, L.Y.1    Sulea, T.2    Szittner, R.3    Vassilyev, V.4    Purisima, E.O.5    Meighen, E.A.6
  • 35
    • 0001757135 scopus 로고
    • Identification of a trisaccharide repeating unit in the enterobacterial common antigen
    • Lugowski, C., E. Romanowska, L. Kenne, and B. Lindberg. 1983. Identification of a trisaccharide repeating unit in the enterobacterial common antigen. Carbohydr. Res. 118:173-181.
    • (1983) Carbohydr. Res. , vol.118 , pp. 173-181
    • Lugowski, C.1    Romanowska, E.2    Kenne, L.3    Lindberg, B.4
  • 36
    • 0017096081 scopus 로고
    • Enterobacterial common antigen
    • Makela, P. H., and H. Mayer. 1976. Enterobacterial common antigen. Bacteriol. Rev. 40:591-632.
    • (1976) Bacteriol. Rev. , vol.40 , pp. 591-632
    • Makela, P.H.1    Mayer, H.2
  • 37
    • 0001420011 scopus 로고
    • Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses
    • Matsuhashi, M., and J. L. Strominger. 1964. Thymidine diphosphate 4-acetamido-4,6-dideoxyhexoses. J. Biol. Chem. 239:2454-2463.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2454-2463
    • Matsuhashi, M.1    Strominger, J.L.2
  • 38
    • 0025076335 scopus 로고
    • Biosynthesis of enterobacterial common antigen in Escherichia coli. Biochemical characterization of Tn10 insertion mutants defective in enterobacterial common antigen synthesis
    • Meier-Dieter, U., R. Starman, K. Barr, H. Mayer, and P. D. Rick. 1990. Biosynthesis of enterobacterial common antigen in Escherichia coli. Biochemical characterization of Tn10 insertion mutants defective in enterobacterial common antigen synthesis. J. Biol. Chem. 265:13490-13497.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13490-13497
    • Meier-Dieter, U.1    Starman, R.2    Barr, K.3    Mayer, H.4    Rick, P.D.5
  • 39
    • 0026595887 scopus 로고
    • Nucleotide sequence of the Escherichia coli rfe gene involved in the synthesis of enterobacterial common antigen. Molecular cloning of the rfe-rff gene cluster
    • Meier-Dieter, U., K. Barr, R. Starman, L. Hatch, and P. D. Rick. 1992. Nucleotide sequence of the Escherichia coli rfe gene involved in the synthesis of enterobacterial common antigen. Molecular cloning of the rfe-rff gene cluster. J. Biol. Chem. 267:746-753.
    • (1992) J. Biol. Chem. , vol.267 , pp. 746-753
    • Meier-Dieter, U.1    Barr, K.2    Starman, R.3    Hatch, L.4    Rick, P.D.5
  • 40
    • 0032898932 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis
    • Mio, T., T. Yamada-Okabe, M. Arisawa, and H. Yamada-Okabe. 1999. Saccharomyces cerevisiae GNA1, an essential gene encoding a novel acetyltransferase involved in UDP-N-acetylglucosamine synthesis. J. Biol. Chem. 274:424-429.
    • (1999) J. Biol. Chem. , vol.274 , pp. 424-429
    • Mio, T.1    Yamada-Okabe, T.2    Arisawa, M.3    Yamada-Okabe, H.4
  • 42
    • 2442440054 scopus 로고    scopus 로고
    • Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: Interactions with acceptor and nucleotide ligands
    • Mulichak, A. M., W. Lu, H. C. Losey, C. T. Walsh, and R. M. Garavito. 2004. Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands. Biochemistry 43:5170-5180.
    • (2004) Biochemistry , vol.43 , pp. 5170-5180
    • Mulichak, A.M.1    Lu, W.2    Losey, H.C.3    Walsh, C.T.4    Garavito, R.M.5
  • 44
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., S. E. Brenner, T. Hubbard, and C. Chothia. 1995. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 45
    • 0030788541 scopus 로고    scopus 로고
    • Extracting protein alignment models from the sequence database
    • Neuwald, A. F., J. S. Liu, D. J. Lipman, and C. E. Lawrence. 1997. Extracting protein alignment models from the sequence database. Nucleic Acids Res. 25:1665-1677.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1665-1677
    • Neuwald, A.F.1    Liu, J.S.2    Lipman, D.J.3    Lawrence, C.E.4
  • 46
    • 0030954208 scopus 로고    scopus 로고
    • GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein
    • Neuwald, A. F., and D. Landsman. 1997. GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein. Trends Biochem. Sci. 22:154-155.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 154-155
    • Neuwald, A.F.1    Landsman, D.2
  • 47
    • 0023378842 scopus 로고
    • The effects of O-antigen character and enterobacterial common antigen content on the in vivo persistence of aromatic-dependent Salmonella sp. live-vaccine strains
    • Nnalue, N. A., and B. A. Stocker. 1987. The effects of O-antigen character and enterobacterial common antigen content on the in vivo persistence of aromatic-dependent Salmonella sp. live-vaccine strains. Microb. Pathog. 3:31-44.
    • (1987) Microb. Pathog. , vol.3 , pp. 31-44
    • Nnalue, N.A.1    Stocker, B.A.2
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 0035844169 scopus 로고    scopus 로고
    • The crystal structures of apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an ammo-sugar N-acetyltransferase
    • Peneff, C., D. Mengin-Lecreulx, and Y. Bourne. 2001. The crystal structures of apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an ammo-sugar N-acetyltransferase. J. Biol. Chem. 276:16328-16334.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16328-16334
    • Peneff, C.1    Mengin-Lecreulx, D.2    Bourne, Y.3
  • 50
    • 0034751710 scopus 로고    scopus 로고
    • Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12
    • Rahman, A., K. Barr, and P. D. Rick. 2001. Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12. J. Bacteriol. 183:6509-6516.
    • (2001) J. Bacteriol. , vol.183 , pp. 6509-6516
    • Rahman, A.1    Barr, K.2    Rick, P.D.3
  • 51
    • 0042890353 scopus 로고    scopus 로고
    • Role for Salmonella enterica enterobacterial common antigen in bile resistance and virulence
    • Ramos-Morales, F., A. I. Prieto, C. R. Beuzon, D. W. Holden, and J. Casadesus. 2003. Role for Salmonella enterica enterobacterial common antigen in bile resistance and virulence. J. Bacteriol. 185:5328-5332.
    • (2003) J. Bacteriol. , vol.185 , pp. 5328-5332
    • Ramos-Morales, F.1    Prieto, A.I.2    Beuzon, C.R.3    Holden, D.W.4    Casadesus, J.5
  • 53
    • 0000160876 scopus 로고    scopus 로고
    • Enterobacterial common antigen and capsular polysaccharides
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). ASM Press, Washington, D.C.
    • Rick, P. D., and R. P. Silver. 1996. Enterobacterial common antigen and capsular polysaccharides, p. 104-122. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 104-122
    • Rick, P.D.1    Silver, R.P.2
  • 54
    • 0031841034 scopus 로고    scopus 로고
    • Characterization of the lipid-carrier involved in the synthesis of enterobacterial common antigen (ECA) and identification of a novel phosphoglyceride in a mutant of Salmonella typhimurium defective in ECA synthesis
    • Rick, P. D., G. L. Hubbard, M. Kitaoka, H. Nagaki, T. Kinoshita, S. Dowd, V. Simplaceanu, and C. Ho. 1998. Characterization of the lipid-carrier involved in the synthesis of enterobacterial common antigen (ECA) and identification of a novel phosphoglyceride in a mutant of Salmonella typhimurium defective in ECA synthesis. Glycobiology 8:557-567.
    • (1998) Glycobiology , vol.8 , pp. 557-567
    • Rick, P.D.1    Hubbard, G.L.2    Kitaoka, M.3    Nagaki, H.4    Kinoshita, T.5    Dowd, S.6    Simplaceanu, V.7    Ho, C.8
  • 55
    • 0038607122 scopus 로고    scopus 로고
    • Evidence that the wzxE gene of Escherichia coli K-12 encodes a protein involved in the transbilayer movement of a trisaccharide-lipid repeat intermediate in the assembly of enterobacterial common antigen
    • Rick, P. D., K. Barr, K. Sankaran, J. Kajimura, J. S. Rush, and C. J. Waechter. 2003. Evidence that the wzxE gene of Escherichia coli K-12 encodes a protein involved in the transbilayer movement of a trisaccharide-lipid repeat intermediate in the assembly of enterobacterial common antigen. J. Biol. Chem. 278:16534-16542.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16534-16542
    • Rick, P.D.1    Barr, K.2    Sankaran, K.3    Kajimura, J.4    Rush, J.S.5    Waechter, C.J.6
  • 56
    • 0018889709 scopus 로고
    • Localization of enterobacterial common antigen: Proteus mirabilis and its various L-forms
    • Rinno, J., J. Gmeiner, J. R. Golecki, and H. Mayer. 1980. Localization of enterobacterial common antigen: Proteus mirabilis and its various L-forms. J. Bacteriol. 141:822-827.
    • (1980) J. Bacteriol. , vol.141 , pp. 822-827
    • Rinno, J.1    Gmeiner, J.2    Golecki, J.R.3    Mayer, H.4
  • 57
    • 0037124069 scopus 로고    scopus 로고
    • Investigation of the roles of catalytic residues in serotonin N-acetyltransferase
    • Scheibner, K. A., J. De Angelis, S. K. Burley, and P. A. Cole. 2002. Investigation of the roles of catalytic residues in serotonin N-acetyltransferase. J. Biol. Chem. 277:18118-18126.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18118-18126
    • Scheibner, K.A.1    De Angelis, J.2    Burley, S.K.3    Cole, P.A.4
  • 60
    • 0027478123 scopus 로고
    • Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes
    • Shaw, K. J., P. N. Rather, R. S. Hare, and G. H. Miller. 1993. Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes. Microbiol. Rev. 57:138-163.
    • (1993) Microbiol. Rev. , vol.57 , pp. 138-163
    • Shaw, K.J.1    Rather, P.N.2    Hare, R.S.3    Miller, G.H.4
  • 61
    • 23044447870 scopus 로고    scopus 로고
    • Crystal structure oiMelhanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI
    • Sivaraman, J., R. S. Meyers, L. Boju, T. Sulea, M. Cygler, J. Davisson, and J. D. Schrag. 2005. Crystal structure oiMelhanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI. Biochemistry 44:10071-10080.
    • (2005) Biochemistry , vol.44 , pp. 10071-10080
    • Sivaraman, J.1    Meyers, R.S.2    Boju, L.3    Sulea, T.4    Cygler, M.5    Davisson, J.6    Schrag, J.D.7
  • 62
    • 0034698085 scopus 로고    scopus 로고
    • Kinetic mechanism of the histone acetyltransferase GCN5 from yeast
    • Tanner, K. G., M. R. Langer, Y. Kim, and J. M. Denu. 2000. Kinetic mechanism of the histone acetyltransferase GCN5 from yeast. J. Biol. Chem. 275:22048-22055.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22048-22055
    • Tanner, K.G.1    Langer, M.R.2    Kim, Y.3    Denu, J.M.4
  • 63
    • 0034601778 scopus 로고    scopus 로고
    • Kinetic mechanism of human histone acetyltransferase P/CAF
    • Tanner, K. G., M. R. Langer, and J. M. Denu. 2000. Kinetic mechanism of human histone acetyltransferase P/CAF. Biochemistry 39:11961-11969.
    • (2000) Biochemistry , vol.39 , pp. 11961-11969
    • Tanner, K.G.1    Langer, M.R.2    Denu, J.M.3
  • 64
    • 0026730661 scopus 로고
    • Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
    • Tercero, J. C., L. E. Riles, and R. B. Wickner. 1992. Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae. J. Biol. Chem. 267:20270-20276.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20270-20276
    • Tercero, J.C.1    Riles, L.E.2    Wickner, R.B.3
  • 66
    • 0346668356 scopus 로고    scopus 로고
    • Structural and kinetic studies of sugar binding to galactose mutarotase from Lactococcus lactis
    • Thoden, J. B., J. Kim, F. M. Raushel, and H. M. Holden. 2002. Structural and kinetic studies of sugar binding to galactose mutarotase from Lactococcus lactis. J. Biol. Chem. 277:45458-45465.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45458-45465
    • Thoden, J.B.1    Kim, J.2    Raushel, F.M.3    Holden, H.M.4
  • 68
    • 0017070607 scopus 로고
    • Effect of enterobacterial common antigen on mouse virulence of Salmonella typhimurium
    • Valtonen, M. V., U. M. Larinkari, M. Plosila, V. V. Valtonen, and P. H. Makela. 1976. Effect of enterobacterial common antigen on mouse virulence of Salmonella typhimurium. Infect. Immun. 13:1601-1605.
    • (1976) Infect. Immun. , vol.13 , pp. 1601-1605
    • Valtonen, M.V.1    Larinkari, U.M.2    Plosila, M.3    Valtonen, V.V.4    Makela, P.H.5
  • 69
    • 0036707544 scopus 로고    scopus 로고
    • Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme a and aminoglycoside substrates
    • Vetting, M. W., S. S. Hegde, F. Javid-Majd, J. S. Blanchard, and S. L. Roderick. 2002. Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nat. Struct. Biol. 9:653-658.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 653-658
    • Vetting, M.W.1    Hegde, S.S.2    Javid-Majd, F.3    Blanchard, J.S.4    Roderick, S.L.5
  • 70
    • 0042511920 scopus 로고    scopus 로고
    • Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases
    • Vetting, M. W., S. L. Roderick, M. Yu, and J. S. Blanchard. 2003. Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases. Protein Sci. 12:1954-1959.
    • (2003) Protein Sci. , vol.12 , pp. 1954-1959
    • Vetting, M.W.1    Roderick, S.L.2    Yu, M.3    Blanchard, J.S.4
  • 71
    • 1942490112 scopus 로고    scopus 로고
    • A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones
    • Vetting, M. W., S. Magnet, E. Nieves, S. L. Roderick, and J. S. Blanchard. 2004. A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones. Chem. Biol. 11:565-573.
    • (2004) Chem. Biol. , vol.11 , pp. 565-573
    • Vetting, M.W.1    Magnet, S.2    Nieves, E.3    Roderick, S.L.4    Blanchard, J.S.5
  • 77
    • 33746597420 scopus 로고
    • Immunological studies of a heterogenetic enterobacterial antigen (Kunin)
    • Whang, H. Y., and E. Neter. 1962. Immunological studies of a heterogenetic enterobacterial antigen (Kunin). J. Bacteriol. 84:1245-1250.
    • (1962) J. Bacteriol. , vol.84 , pp. 1245-1250
    • Whang, H.Y.1    Neter, E.2
  • 79
    • 0036299021 scopus 로고    scopus 로고
    • X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition
    • Wolf, E., J. De Angelis, E. M. Khalil, P. A. Cole, and S. K. Burley. 2002. X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition. J. Mol. Biol. 317:215-224.
    • (2002) J. Mol. Biol. , vol.317 , pp. 215-224
    • Wolf, E.1    De Angelis, J.2    Khalil, E.M.3    Cole, P.A.4    Burley, S.K.5
  • 80
    • 0033135707 scopus 로고    scopus 로고
    • Crystal structure of an aminoglycoside 6′-N-acetyltransferase: Defining the GCN5-related N-acetyltransferase superfamily fold
    • Wybenga-Groot, L. E., K. Draker, G. D. Wright, and A. M. Berghuis. 1999. Crystal structure of an aminoglycoside 6′-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold. Structure 7:497-507.
    • (1999) Structure , vol.7 , pp. 497-507
    • Wybenga-Groot, L.E.1    Draker, K.2    Wright, G.D.3    Berghuis, A.M.4


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