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Volumn 14, Issue 9, 2006, Pages 1425-1435

FeeM, an N-Acyl Amino Acid Synthase from an Uncultured Soil Microbe: Structure, Mechanism, and Acyl Carrier Protein Binding

Author keywords

[No Author keywords available]

Indexed keywords

ACYL CARRIER PROTEIN; ACYLTRANSFERASE; DNA; HISTONE ACETYLTRANSFERASE GCN5; HYDROGEN; SYNTHETASE;

EID: 33748328250     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.07.005     Document Type: Article
Times cited : (31)

References (65)
  • 1
    • 0001763933 scopus 로고    scopus 로고
    • Difference structure factor normalization for heavy-atom or anomalous-scattering substructure determinations
    • Blessing R.H., and Smith G.D. Difference structure factor normalization for heavy-atom or anomalous-scattering substructure determinations. J. Appl. Crystallogr. 32 (1999) 664-670
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 664-670
    • Blessing, R.H.1    Smith, G.D.2
  • 2
    • 0034722959 scopus 로고    scopus 로고
    • Long-chain N-acyl amino acid antibiotics isolated from heterologously expressed environmental DNA
    • Brady S.F., and Clardy J. Long-chain N-acyl amino acid antibiotics isolated from heterologously expressed environmental DNA. J. Am. Chem. Soc. 122 (2000) 12903-12904
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12903-12904
    • Brady, S.F.1    Clardy, J.2
  • 3
    • 4344625255 scopus 로고    scopus 로고
    • Palmitoylputrescine, an antibiotic isolated from the heterologous expression of DNA extracted from bromeliad tank water
    • Brady S.F., and Clardy J. Palmitoylputrescine, an antibiotic isolated from the heterologous expression of DNA extracted from bromeliad tank water. J. Nat. Prod. 67 (2004) 1283-1286
    • (2004) J. Nat. Prod. , vol.67 , pp. 1283-1286
    • Brady, S.F.1    Clardy, J.2
  • 4
    • 27744453364 scopus 로고    scopus 로고
    • Cloning and heterologous expression of isocyanide biosynthetic genes from environmental DNA
    • Brady S.F., and Clardy J. Cloning and heterologous expression of isocyanide biosynthetic genes from environmental DNA. Angew. Chem. Int. Ed. Engl. 44 (2005) 7063-7065
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 7063-7065
    • Brady, S.F.1    Clardy, J.2
  • 5
    • 24044517824 scopus 로고    scopus 로고
    • N-acyl derivatives of arginine and tryptophan isolated from environmental DNA expressed in Escherichia coli
    • Brady S.F., and Clardy J. N-acyl derivatives of arginine and tryptophan isolated from environmental DNA expressed in Escherichia coli. Org. Lett. 7 (2005) 3613-3616
    • (2005) Org. Lett. , vol.7 , pp. 3613-3616
    • Brady, S.F.1    Clardy, J.2
  • 6
    • 27744497479 scopus 로고    scopus 로고
    • Systematic investigation of the Escherichia coli metabolome for the biosynthetic origin of an isocyanide carbon atom
    • Brady S.F., and Clardy J. Systematic investigation of the Escherichia coli metabolome for the biosynthetic origin of an isocyanide carbon atom. Angew. Chem. Int. Ed. Engl. 44 (2005) 7045-7048
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 7045-7048
    • Brady, S.F.1    Clardy, J.2
  • 7
    • 0035963668 scopus 로고    scopus 로고
    • Cloning and heterologous expression of a natural product biosynthetic gene cluster from eDNA
    • Brady S.F., Chao C.J., Handelsman J., and Clardy J. Cloning and heterologous expression of a natural product biosynthetic gene cluster from eDNA. Org. Lett. 3 (2001) 1981-1984
    • (2001) Org. Lett. , vol.3 , pp. 1981-1984
    • Brady, S.F.1    Chao, C.J.2    Handelsman, J.3    Clardy, J.4
  • 8
    • 0037189889 scopus 로고    scopus 로고
    • New natural product families from an environmental DNA (eDNA) gene cluster
    • Brady S.F., Chao C.J., and Clardy J. New natural product families from an environmental DNA (eDNA) gene cluster. J. Am. Chem. Soc. 124 (2002) 9968-9969
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9968-9969
    • Brady, S.F.1    Chao, C.J.2    Clardy, J.3
  • 9
    • 8744289725 scopus 로고    scopus 로고
    • Long-chain N-acyltyrosine synthases from environmental DNA
    • Brady S.F., Chao C.J., and Clardy J. Long-chain N-acyltyrosine synthases from environmental DNA. Appl. Environ. Microbiol. 70 (2004) 6865-6870
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 6865-6870
    • Brady, S.F.1    Chao, C.J.2    Clardy, J.3
  • 10
    • 0026597444 scopus 로고
    • Free R-value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R-value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 11
    • 0001568088 scopus 로고
    • XDL VIEW, an X-windows-based toolkit for crystallographic and other applications
    • Campbell J.W. XDL VIEW, an X-windows-based toolkit for crystallographic and other applications. J. Appl. Crystallogr. 28 (1995) 236-242
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 236-242
    • Campbell, J.W.1
  • 12
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 14
    • 11144311139 scopus 로고    scopus 로고
    • Lessons from natural molecules
    • Clardy J., and Walsh C.T. Lessons from natural molecules. Nature 432 (2004) 829-837
    • (2004) Nature , vol.432 , pp. 829-837
    • Clardy, J.1    Walsh, C.T.2
  • 15
    • 0033168714 scopus 로고    scopus 로고
    • Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
    • Clements A., Rojas J.R., Trievel R.C., Wang L., Berger S.L., and Marmorstein R. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. EMBO J. 18 (1999) 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
  • 16
    • 0002583957 scopus 로고
    • DM: an automated procedure for phase improvement by density modification
    • Cowtan K. DM: an automated procedure for phase improvement by density modification. CCP4/ESF-EACBM Newsl. Protein Crystallogr. 31 (1994) 34-38
    • (1994) CCP4/ESF-EACBM Newsl. Protein Crystallogr. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 18
    • 0032579377 scopus 로고    scopus 로고
    • Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87)
    • De Angelis J., Gastel J., Klein D.C., and Cole P.A. Kinetic analysis of the catalytic mechanism of serotonin N-acetyltransferase (EC 2.3.1.87). J. Biol. Chem. 273 (1998) 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
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle E., and Bricogne G. Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276 (1997) 472-494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • de La Fortelle, E.1    Bricogne, G.2
  • 21
    • 0347093476 scopus 로고    scopus 로고
    • Molecular mechanism of the enterococcal aminoglycoside 6′-N-acetyltransferase: role of GNAT-conserved residues in the chemistry of antibiotic inactivation
    • Draker K.A., and Wright G.D. Molecular mechanism of the enterococcal aminoglycoside 6′-N-acetyltransferase: role of GNAT-conserved residues in the chemistry of antibiotic inactivation. Biochemistry 43 (2004) 446-454
    • (2004) Biochemistry , vol.43 , pp. 446-454
    • Draker, K.A.1    Wright, G.D.2
  • 24
    • 0035822617 scopus 로고    scopus 로고
    • Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis
    • Farazi T.A., Manchester J.K., Waksman G., and Gordon J.I. Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis. Biochemistry 40 (2001) 9177-9186
    • (2001) Biochemistry , vol.40 , pp. 9177-9186
    • Farazi, T.A.1    Manchester, J.K.2    Waksman, G.3    Gordon, J.I.4
  • 25
    • 0000952473 scopus 로고
    • On the treatment of negative intensity observations
    • French S., and Wilson K. On the treatment of negative intensity observations. Acta Crystallogr. A 34 (1978) 517-525
    • (1978) Acta Crystallogr. A , vol.34 , pp. 517-525
    • French, S.1    Wilson, K.2
  • 26
    • 0037168560 scopus 로고    scopus 로고
    • Transcriptional modulation of bacterial gene expression by subinhibitory concentrations of antibiotics
    • Goh E.B., Yim G., Tsui W., McClure J., Surette M.G., and Davies J. Transcriptional modulation of bacterial gene expression by subinhibitory concentrations of antibiotics. Proc. Natl. Acad. Sci. USA 99 (2002) 17025-17030
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 17025-17030
    • Goh, E.B.1    Yim, G.2    Tsui, W.3    McClure, J.4    Surette, M.G.5    Davies, J.6
  • 27
    • 4344612832 scopus 로고    scopus 로고
    • Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI
    • Gould T.A., Schweizer H.P., and Churchill M.E. Structure of the Pseudomonas aeruginosa acyl-homoserinelactone synthase LasI. Mol. Microbiol. 53 (2004) 1135-1146
    • (2004) Mol. Microbiol. , vol.53 , pp. 1135-1146
    • Gould, T.A.1    Schweizer, H.P.2    Churchill, M.E.3
  • 28
    • 0034846215 scopus 로고    scopus 로고
    • Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems
    • Guerrero S.A., Hecht H.J., Hofmann B., Biebl H., and Singh M. Production of selenomethionine-labelled proteins using simplified culture conditions and generally applicable host/vector systems. Appl. Microbiol. Biotechnol. 56 (2001) 718-723
    • (2001) Appl. Microbiol. Biotechnol. , vol.56 , pp. 718-723
    • Guerrero, S.A.1    Hecht, H.J.2    Hofmann, B.3    Biebl, H.4    Singh, M.5
  • 29
    • 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., Namboodiri M.A., Klein D.C., and Dyda F. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 Å resolution with a bisubstrate analog. Cell 97 (1999) 361-369
    • (1999) Cell , vol.97 , pp. 361-369
    • Hickman, A.B.1    Namboodiri, M.A.2    Klein, D.C.3    Dyda, F.4
  • 30
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 31
    • 0032879027 scopus 로고    scopus 로고
    • Forty years of genetics with Streptomyces: from in vivo through in vitro to in silico
    • Hopwood D.A. Forty years of genetics with Streptomyces: from in vivo through in vitro to in silico. Microbiology 145 (1999) 2183-2202
    • (1999) Microbiology , vol.145 , pp. 2183-2202
    • Hopwood, D.A.1
  • 32
    • 0031662188 scopus 로고    scopus 로고
    • Impact of culture-independent studies on the emerging phylogenetic view of bacterial diversity
    • Hugenholtz P., Goebel B.M., and Pace N.R. Impact of culture-independent studies on the emerging phylogenetic view of bacterial diversity. J. Bacteriol. 180 (1998) 4765-4774
    • (1998) J. Bacteriol. , vol.180 , pp. 4765-4774
    • Hugenholtz, P.1    Goebel, B.M.2    Pace, N.R.3
  • 33
    • 0002552477 scopus 로고
    • *? A set of averaging programs
    • Dodson E.J., Glover S., and Wolf W. (Eds), Daresbury Laboratory, Warrington, UK
    • *? A set of averaging programs. In: Dodson E.J., Glover S., and Wolf W. (Eds). Molecular Replacement (1992), Daresbury Laboratory, Warrington, UK 91-105
    • (1992) Molecular Replacement , pp. 91-105
    • Jones, T.A.1
  • 34
    • 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., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 35
    • 0002700643 scopus 로고
    • Halloween...masks and bones
    • Bailey S., Hubbard R., and Waller D.A. (Eds), Daresbury Laboratory, Warrington, UK
    • Kleywegt G.J., and Jones T.A. Halloween...masks and bones. In: Bailey S., Hubbard R., and Waller D.A. (Eds). From First Map to Final Model (1994), Daresbury Laboratory, Warrington, UK 59-66
    • (1994) From First Map to Final Model , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 37
    • 0030498233 scopus 로고    scopus 로고
    • xdlMAPMAN and xdlDATAMAN-programs for reformatting and manipulation of biomacromolecular electron-density maps and reflection data sets
    • Kleywegt G.J., and Jones T.A. xdlMAPMAN and xdlDATAMAN-programs for reformatting and manipulation of biomacromolecular electron-density maps and reflection data sets. Acta Crystallogr. D Biol. Crystallogr. 52 (1996) 826-828
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 42
    • 21044448952 scopus 로고    scopus 로고
    • Daptomycin biosynthesis in Streptomyces roseosporus: cloning and analysis of the gene cluster and revision of peptide stereochemistry
    • Miao V., Coeffet-Legal M.F., Brian P., Brost R., Penn J., Whiting A., Martin S., Ford R., Parr I., Bouchard M., et al. Daptomycin biosynthesis in Streptomyces roseosporus: cloning and analysis of the gene cluster and revision of peptide stereochemistry. Microbiology 151 (2005) 1507-1523
    • (2005) Microbiology , vol.151 , pp. 1507-1523
    • Miao, V.1    Coeffet-Legal, M.F.2    Brian, P.3    Brost, R.4    Penn, J.5    Whiting, A.6    Martin, S.7    Ford, R.8    Parr, I.9    Bouchard, M.10
  • 45
    • 0030982247 scopus 로고    scopus 로고
    • A molecular view of microbial diversity and the biosphere
    • Pace N.R. A molecular view of microbial diversity and the biosphere. Science 276 (1997) 734-740
    • (1997) Science , vol.276 , pp. 734-740
    • Pace, N.R.1
  • 46
    • 0034662753 scopus 로고    scopus 로고
    • Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites
    • Parris K.D., Lin L., Tam A., Mathew R., Hixon J., Stahl M., Fritz C.C., Seehra J., and Somers W.S. Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Struct. Fold. Des. 8 (2000) 883-895
    • (2000) Struct. Fold. Des. , vol.8 , pp. 883-895
    • Parris, K.D.1    Lin, L.2    Tam, A.3    Mathew, R.4    Hixon, J.5    Stahl, M.6    Fritz, C.C.7    Seehra, J.8    Somers, W.S.9
  • 47
    • 0027299747 scopus 로고
    • Expression of Pseudomonas aeruginosa virulence genes requires cell-to-cell communication
    • Passador L., Cook J.M., Gambello M.J., Rust L., and Iglewski B.H. Expression of Pseudomonas aeruginosa virulence genes requires cell-to-cell communication. Science 260 (1993) 1127-1130
    • (1993) Science , vol.260 , pp. 1127-1130
    • Passador, L.1    Cook, J.M.2    Gambello, M.J.3    Rust, L.4    Iglewski, B.H.5
  • 48
    • 0035844169 scopus 로고    scopus 로고
    • The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase
    • Peneff C., Mengin-Lecreulx D., and Bourne Y. The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase. J. Biol. Chem. 276 (2001) 16328-16334
    • (2001) J. Biol. Chem. , vol.276 , pp. 16328-16334
    • Peneff, C.1    Mengin-Lecreulx, D.2    Bourne, Y.3
  • 49
    • 0031214792 scopus 로고    scopus 로고
    • 6-tag and maltose-binding-protein double-affinity fusion system
    • 6-tag and maltose-binding-protein double-affinity fusion system. Protein Expr. Purif. 10 (1997) 309-319
    • (1997) Protein Expr. Purif. , vol.10 , pp. 309-319
    • Pryor, K.D.1    Leiting, B.2
  • 50
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • Quadri L.E., Weinreb P.H., Lei M., Nakano M.M., Zuber P., and Walsh C.T. Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases. Biochemistry 37 (1998) 1585-1595
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.1    Weinreb, P.H.2    Lei, M.3    Nakano, M.M.4    Zuber, P.5    Walsh, C.T.6
  • 52
    • 0027049243 scopus 로고
    • The kinemage: a tool for scientific communication
    • Richardson D.C., and Richardson J.S. The kinemage: a tool for scientific communication. Protein Sci. 1 (1992) 3-9
    • (1992) Protein Sci. , vol.1 , pp. 3-9
    • Richardson, D.C.1    Richardson, J.S.2
  • 55
    • 0037124069 scopus 로고    scopus 로고
    • Investigation of the roles of catalytic residues in serotonin N-acetyltransferase
    • Scheibner K.A., De Angelis J., Burley S.K., and Cole P.A. Investigation of the roles of catalytic residues in serotonin N-acetyltransferase. J. Biol. Chem. 277 (2002) 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
  • 56
    • 0001841380 scopus 로고
    • On the rigid-body motion of molecules in crystals
    • Schomaker V., and Trueblood K.N. On the rigid-body motion of molecules in crystals. Acta Crystallogr. B 24 (1968) 63-76
    • (1968) Acta Crystallogr. B , vol.24 , pp. 63-76
    • Schomaker, V.1    Trueblood, K.N.2
  • 57
    • 0029899872 scopus 로고    scopus 로고
    • Induction of phenazine biosynthesis in cultures of Pseudomonas aeruginosa by L-N-(3-oxohexanoyl)homoserine lactone
    • Stead P., Rudd B.A., Bradshaw H., Noble D., and Dawson M.J. Induction of phenazine biosynthesis in cultures of Pseudomonas aeruginosa by L-N-(3-oxohexanoyl)homoserine lactone. FEMS Microbiol. Lett. 140 (1996) 15-22
    • (1996) FEMS Microbiol. Lett. , vol.140 , pp. 15-22
    • Stead, P.1    Rudd, B.A.2    Bradshaw, H.3    Noble, D.4    Dawson, M.J.5
  • 58
    • 0000614826 scopus 로고    scopus 로고
    • An algorithm for automatic indexing of oscillation images using Fourier analysis
    • Steller I., Bolotovsky R., and Rossmann M.G. An algorithm for automatic indexing of oscillation images using Fourier analysis. J. Appl. Crystallogr. 30 (1997) 1036-1040
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1036-1040
    • Steller, I.1    Bolotovsky, R.2    Rossmann, M.G.3
  • 59
    • 0033603555 scopus 로고    scopus 로고
    • Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator
    • Tanner K.G., Trievel R.C., Kuo M.H., Howard R.M., Berger S.L., Allis C.D., Marmorstein R., and Denu J.M. Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator. J. Biol. Chem. 274 (1999) 18157-18160
    • (1999) J. Biol. Chem. , vol.274 , pp. 18157-18160
    • Tanner, K.G.1    Trievel, R.C.2    Kuo, M.H.3    Howard, R.M.4    Berger, S.L.5    Allis, C.D.6    Marmorstein, R.7    Denu, J.M.8
  • 60
    • 0036270789 scopus 로고    scopus 로고
    • Microbial diversity and function in soil: from genes to ecosystems
    • Torsvik V., and Øvreås L. Microbial diversity and function in soil: from genes to ecosystems. Curr. Opin. Microbiol. 5 (2002) 240-245
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 240-245
    • Torsvik, V.1    Øvreås, L.2
  • 61
    • 0031923690 scopus 로고    scopus 로고
    • In vivo evidence that S-adenosylmethionine and fatty acid synthesis intermediates are the substrates for the LuxI family of autoinducer synthases
    • Val D.L., and Cronan Jr. J.E. In vivo evidence that S-adenosylmethionine and fatty acid synthesis intermediates are the substrates for the LuxI family of autoinducer synthases. J. Bacteriol. 180 (1998) 2644-2651
    • (1998) J. Bacteriol. , vol.180 , pp. 2644-2651
    • Val, D.L.1    Cronan Jr., J.E.2
  • 62
    • 0036204586 scopus 로고    scopus 로고
    • Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing
    • Watson W.T., Minogue T.D., Val D.L., von Bodman S.B., and Churchill M.E. Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing. Mol. Cell 9 (2002) 685-694
    • (2002) Mol. Cell , vol.9 , pp. 685-694
    • Watson, W.T.1    Minogue, T.D.2    Val, D.L.3    von Bodman, S.B.4    Churchill, M.E.5
  • 63
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks C.M., and Miller R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32 (1999) 120-124
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 65
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word J.M., Lovell S.C., Richardson J.S., and Richardson D.C. Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol. 285 (1999) 1735-1747
    • (1999) J. Mol. Biol. , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4


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