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Volumn 389, Issue 3, 2009, Pages 511-528

Probing the Interactions of Early Polyketide Intermediates with the Actinorhodin ACP from S. coelicolor A3(2)

Author keywords

acyl carrier protein; conformational switching; NMR structure; polyketide binding; polyketide biosynthesis

Indexed keywords

ACTINORHODINE; ACYL CARRIER PROTEIN; ALANINE; BUTYRIC ACID DERIVATIVE; HEXANOIC ACID DERIVATIVE; LEUCINE; OCTANOIC ACID DERIVATIVE; POLYKETIDE; THREONINE;

EID: 65649101867     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.03.072     Document Type: Article
Times cited : (48)

References (61)
  • 1
    • 0027024882 scopus 로고
    • Genes for polyketide secondary metabolic pathways in microorganisms and plants
    • Hopwood D.A., and Khosla C. Genes for polyketide secondary metabolic pathways in microorganisms and plants. Ciba Found. Symp. 171 (1992) 88-112
    • (1992) Ciba Found. Symp. , vol.171 , pp. 88-112
    • Hopwood, D.A.1    Khosla, C.2
  • 2
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: a millennium review
    • Staunton J., and Weissman K.J. Polyketide biosynthesis: a millennium review. Nat. Prod. Rep. 18 (2001) 380-416
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 3
    • 33846923183 scopus 로고    scopus 로고
    • Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork
    • Hertweck C., Luzhetskyy A., Rebets Y., and Bechthold A. Type II polyketide synthases: gaining a deeper insight into enzymatic teamwork. Nat. Prod. Rep. 24 (2007) 162-190
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 162-190
    • Hertweck, C.1    Luzhetskyy, A.2    Rebets, Y.3    Bechthold, A.4
  • 4
    • 34848843433 scopus 로고    scopus 로고
    • The type I fatty acid and polyketide synthases: a tale of two megasynthases
    • Smith S., and Tsai S.C. The type I fatty acid and polyketide synthases: a tale of two megasynthases. Nat. Prod. Rep. 24 (2007) 1041-1072
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 1041-1072
    • Smith, S.1    Tsai, S.C.2
  • 5
    • 0030972114 scopus 로고    scopus 로고
    • Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2)
    • Crump M.P., Crosby J., Dempsey C.E., Parkinson J.A., Murray M., Hopwood D.A., and Simpson T.J. Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2). Biochemistry 36 (1997) 6000-6008
    • (1997) Biochemistry , vol.36 , pp. 6000-6008
    • Crump, M.P.1    Crosby, J.2    Dempsey, C.E.3    Parkinson, J.A.4    Murray, M.5    Hopwood, D.A.6    Simpson, T.J.7
  • 6
    • 0038457084 scopus 로고    scopus 로고
    • Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus
    • Findlow S.C., Winsor C., Simpson T.J., Crosby J., and Crump M.P. Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus. Biochemistry 42 (2003) 8423-8433
    • (2003) Biochemistry , vol.42 , pp. 8423-8433
    • Findlow, S.C.1    Winsor, C.2    Simpson, T.J.3    Crosby, J.4    Crump, M.P.5
  • 7
    • 0037472114 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein
    • Li Q., Khosla C., Puglisi J.D., and Liu C.W. Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein. Biochemistry 42 (2003) 4648-4657
    • (2003) Biochemistry , vol.42 , pp. 4648-4657
    • Li, Q.1    Khosla, C.2    Puglisi, J.D.3    Liu, C.W.4
  • 8
    • 54349095025 scopus 로고    scopus 로고
    • An ACP structural switch. Conformational differences between the apo and holo forms of the actinorhodin polyketide synthase acyl carrier protein
    • Evans S.E., Williams C., Arthur C.J., Burston S.G., Simpson T.J., Crosby J., and Crump M.P. An ACP structural switch. Conformational differences between the apo and holo forms of the actinorhodin polyketide synthase acyl carrier protein. ChemBioChem 9 (2008) 2424-2432
    • (2008) ChemBioChem , vol.9 , pp. 2424-2432
    • Evans, S.E.1    Williams, C.2    Arthur, C.J.3    Burston, S.G.4    Simpson, T.J.5    Crosby, J.6    Crump, M.P.7
  • 10
    • 4644370904 scopus 로고    scopus 로고
    • The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding
    • Hadfield A.T., Limpkin C., Teartasin W., Simpson T.J., Crosby J., and Crump M.P. The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding. Structure 12 (2004) 1865-1875
    • (2004) Structure , vol.12 , pp. 1865-1875
    • Hadfield, A.T.1    Limpkin, C.2    Teartasin, W.3    Simpson, T.J.4    Crosby, J.5    Crump, M.P.6
  • 11
    • 8744305865 scopus 로고    scopus 로고
    • Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity
    • Korman T.P., Hill J.A., Vu T.N., and Tsai S.C. Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity. Biochemistry 43 (2004) 14529-14538
    • (2004) Biochemistry , vol.43 , pp. 14529-14538
    • Korman, T.P.1    Hill, J.A.2    Vu, T.N.3    Tsai, S.C.4
  • 12
    • 44449157594 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of tetracenomycin ARO/CYC: implications for cyclization specificity of aromatic polyketides
    • Ames B.D., Korman T.P., Zhang W.J., Smith P., Vu T., Tang Y., and Tsai S.C. Crystal structure and functional analysis of tetracenomycin ARO/CYC: implications for cyclization specificity of aromatic polyketides. Proc. Natl Acad. Sci. USA 105 (2008) 5349-5354
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 5349-5354
    • Ames, B.D.1    Korman, T.P.2    Zhang, W.J.3    Smith, P.4    Vu, T.5    Tang, Y.6    Tsai, S.C.7
  • 13
    • 0037439266 scopus 로고    scopus 로고
    • The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis
    • Sciara G., Kendrew S.G., Miele A.E., Marsh N.G., Federici L., Malatesta F., et al. The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis. EMBO J. 22 (2003) 205-215
    • (2003) EMBO J. , vol.22 , pp. 205-215
    • Sciara, G.1    Kendrew, S.G.2    Miele, A.E.3    Marsh, N.G.4    Federici, L.5    Malatesta, F.6
  • 14
    • 0036848668 scopus 로고    scopus 로고
    • Crystal structure of the priming β-ketosynthase from the R1128 polyketide biosynthetic pathway
    • Pan H., Tsai S.C., Meadows E.S., Miercke L.J.W., Keatinge-Clay A.T., O'Connell J., et al. Crystal structure of the priming β-ketosynthase from the R1128 polyketide biosynthetic pathway. Structure 10 (2002) 1559-1568
    • (2002) Structure , vol.10 , pp. 1559-1568
    • Pan, H.1    Tsai, S.C.2    Meadows, E.S.3    Miercke, L.J.W.4    Keatinge-Clay, A.T.5    O'Connell, J.6
  • 15
    • 0033619244 scopus 로고    scopus 로고
    • A chain initiation factor common to both modular and aromatic polyketide synthases
    • Bisang C., Long P.F., Cortes J., Westcott J., Crosby J., Matharu A.L., et al. A chain initiation factor common to both modular and aromatic polyketide synthases. Nature 401 (1999) 502-505
    • (1999) Nature , vol.401 , pp. 502-505
    • Bisang, C.1    Long, P.F.2    Cortes, J.3    Westcott, J.4    Crosby, J.5    Matharu, A.L.6
  • 16
    • 37249075864 scopus 로고    scopus 로고
    • Dissecting the component reactions catalyzed by the actinorhodin minimal polyketide synthase
    • Beltran-Alvarez P., Cox R.J., Crosby J., and Simpson T.J. Dissecting the component reactions catalyzed by the actinorhodin minimal polyketide synthase. Biochemistry 46 (2007) 14672-14681
    • (2007) Biochemistry , vol.46 , pp. 14672-14681
    • Beltran-Alvarez, P.1    Cox, R.J.2    Crosby, J.3    Simpson, T.J.4
  • 17
    • 0035846645 scopus 로고    scopus 로고
    • In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase
    • Meadows E.S., and Khosla C. In vitro reconstitution and analysis of the chain initiating enzymes of the R1128 polyketide synthase. Biochemistry 40 (2001) 14855-14861
    • (2001) Biochemistry , vol.40 , pp. 14855-14861
    • Meadows, E.S.1    Khosla, C.2
  • 18
    • 0032766245 scopus 로고    scopus 로고
    • The Streptomyces peucetius dpsC gene determines the choice of starter unit in biosynthesis of the daunorubicin polyketide
    • Bao W.L., Sheldon P.J., Wendt-Pienkowsi E., and Hutchinson C.R. The Streptomyces peucetius dpsC gene determines the choice of starter unit in biosynthesis of the daunorubicin polyketide. J. Bacteriol. 181 (1999) 4690-4695
    • (1999) J. Bacteriol. , vol.181 , pp. 4690-4695
    • Bao, W.L.1    Sheldon, P.J.2    Wendt-Pienkowsi, E.3    Hutchinson, C.R.4
  • 19
    • 0037459418 scopus 로고    scopus 로고
    • First in vitro directed biosynthesis of new compounds by a minimal type II polyketide synthase: evidence for the mechanism of chain length determination
    • Nicholson T.P., Winfield C., Westcott J., Crosby J., Simpson T.J., and Cox R.J. First in vitro directed biosynthesis of new compounds by a minimal type II polyketide synthase: evidence for the mechanism of chain length determination. Chem. Commun. (2003) 686-687
    • (2003) Chem. Commun. , pp. 686-687
    • Nicholson, T.P.1    Winfield, C.2    Westcott, J.3    Crosby, J.4    Simpson, T.J.5    Cox, R.J.6
  • 20
    • 22244466130 scopus 로고    scopus 로고
    • The structural biology of type II fatty acid biosynthesis
    • White S.W., Zheng J., Zhang Y.M., and Rock C.O. The structural biology of type II fatty acid biosynthesis. Annu. Rev. Biochem. 74 (2005) 791-831
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 791-831
    • White, S.W.1    Zheng, J.2    Zhang, Y.M.3    Rock, C.O.4
  • 21
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock C.O., and Cronan J.E. Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta 1302 (1996) 1-16
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan, J.E.2
  • 22
    • 0035896547 scopus 로고    scopus 로고
    • Identification and analysis of the acyl carrier protein (ACP) docking site on β-ketoacyl-ACP synthase III
    • Zhang Y.M., Rao M.S., Heath R.J., Price A.C., Olson A.J., Rock C.O., and White S.W. Identification and analysis of the acyl carrier protein (ACP) docking site on β-ketoacyl-ACP synthase III. J. Biol. Chem. 276 (2001) 8231-8238
    • (2001) J. Biol. Chem. , vol.276 , pp. 8231-8238
    • Zhang, Y.M.1    Rao, M.S.2    Heath, R.J.3    Price, A.C.4    Olson, A.J.5    Rock, C.O.6    White, S.W.7
  • 23
    • 34547672758 scopus 로고    scopus 로고
    • Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat
    • Pemble C.W., Johnson L.C., Kridel S.J., and Lowther W.T. Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nat. Struct. Mol. Biol. 14 (2007) 704-709
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 704-709
    • Pemble, C.W.1    Johnson, L.C.2    Kridel, S.J.3    Lowther, W.T.4
  • 24
    • 0037314870 scopus 로고    scopus 로고
    • Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase
    • Keatinge-Clay A.T., Shelat A.A., Savage D.F., Tsai S.C., Miercke L.J.W., O'Connell J.D., et al. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase. Structure 11 (2003) 147-154
    • (2003) Structure , vol.11 , pp. 147-154
    • Keatinge-Clay, A.T.1    Shelat, A.A.2    Savage, D.F.3    Tsai, S.C.4    Miercke, L.J.W.5    O'Connell, J.D.6
  • 25
    • 0042542833 scopus 로고
    • Biomimetic syntheses of aromatic polyketide metabolites
    • Harris T.M., and Harris C.M. Biomimetic syntheses of aromatic polyketide metabolites. Pure Appl. Chem. 58 (1986) 283-294
    • (1986) Pure Appl. Chem. , vol.58 , pp. 283-294
    • Harris, T.M.1    Harris, C.M.2
  • 26
    • 0036277954 scopus 로고    scopus 로고
    • X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site
    • Roujeinikova A., Baldock C., Simon W.J., Gilroy J., Baker P.J., Stuitje A.R., et al. X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site. Structure 10 (2002) 825-835
    • (2002) Structure , vol.10 , pp. 825-835
    • Roujeinikova, A.1    Baldock, C.2    Simon, W.J.3    Gilroy, J.4    Baker, P.J.5    Stuitje, A.R.6
  • 27
    • 33751512907 scopus 로고    scopus 로고
    • Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates
    • Roujeinikova A., Simon W.J., Gilroy J., Rice D.W., Rafferty J.B., and Slabas A.R. Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates. J. Mol. Biol. 365 (2007) 135-145
    • (2007) J. Mol. Biol. , vol.365 , pp. 135-145
    • Roujeinikova, A.1    Simon, W.J.2    Gilroy, J.3    Rice, D.W.4    Rafferty, J.B.5    Slabas, A.R.6
  • 28
    • 33645968397 scopus 로고    scopus 로고
    • Solution structures of spinach acyl carrier protein with decanoate and stearate
    • Zornetzer G.A., Fox B.G., and Markley J.L. Solution structures of spinach acyl carrier protein with decanoate and stearate. Biochemistry 45 (2006) 5217-5227
    • (2006) Biochemistry , vol.45 , pp. 5217-5227
    • Zornetzer, G.A.1    Fox, B.G.2    Markley, J.L.3
  • 29
    • 31744434177 scopus 로고    scopus 로고
    • NMR studies of Escherichia coli acyl carrier protein: dynamic and structural differences of the apo- and holo-forms
    • Kim Y., Kovrigin E.L., and Eletr Z. NMR studies of Escherichia coli acyl carrier protein: dynamic and structural differences of the apo- and holo-forms. Biochem. Biophys. Res. Commun. 341 (2006) 776-783
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 776-783
    • Kim, Y.1    Kovrigin, E.L.2    Eletr, Z.3
  • 30
    • 33645807617 scopus 로고    scopus 로고
    • Conformational switches modulate protein interactions in peptide antibiotic synthetases
    • Koglin A., Mofid M.R., Löhr F., Schäfer B., Rogov V.V., Blum M.M., et al. Conformational switches modulate protein interactions in peptide antibiotic synthetases. Science 312 (2006) 273-276
    • (2006) Science , vol.312 , pp. 273-276
    • Koglin, A.1    Mofid, M.R.2    Löhr, F.3    Schäfer, B.4    Rogov, V.V.5    Blum, M.M.6
  • 31
    • 0021238139 scopus 로고
    • Molecular cloning of the whole biosynthetic pathway of a Streptomyces antibiotic and its expression in a heterologous host
    • Malpartida F., and Hopwood D.A. Molecular cloning of the whole biosynthetic pathway of a Streptomyces antibiotic and its expression in a heterologous host. Nature 309 (1984) 462-464
    • (1984) Nature , vol.309 , pp. 462-464
    • Malpartida, F.1    Hopwood, D.A.2
  • 32
    • 0030936596 scopus 로고    scopus 로고
    • Post-translational modification of heterologously expressed Streptomyces type II polyketide synthase acyl carrier proteins
    • Cox R.J., Hitchman T.S., Byrom K.J., Findlow I.S.C., Tanner J.A., Crosby J., and Simpson T.J. Post-translational modification of heterologously expressed Streptomyces type II polyketide synthase acyl carrier proteins. FEBS Lett. 405 (1997) 267-272
    • (1997) FEBS Lett. , vol.405 , pp. 267-272
    • Cox, R.J.1    Hitchman, T.S.2    Byrom, K.J.3    Findlow, I.S.C.4    Tanner, J.A.5    Crosby, J.6    Simpson, T.J.7
  • 33
    • 0036523469 scopus 로고    scopus 로고
    • Synthesis and characterisation of acyl carrier protein bound polyketide analogues
    • Arthur C., Cox R.J., Crosby J., Rahman M.M., Simpson T.J., Soulas F., et al. Synthesis and characterisation of acyl carrier protein bound polyketide analogues. ChemBioChem 3 (2002) 253-257
    • (2002) ChemBioChem , vol.3 , pp. 253-257
    • Arthur, C.1    Cox, R.J.2    Crosby, J.3    Rahman, M.M.4    Simpson, T.J.5    Soulas, F.6
  • 34
    • 1242340502 scopus 로고    scopus 로고
    • New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes
    • Peterson R.D., Theimer C.A., Wu H.H., and Feigon J. New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes. J. Biomol. NMR 28 (2004) 59-67
    • (2004) J. Biomol. NMR , vol.28 , pp. 59-67
    • Peterson, R.D.1    Theimer, C.A.2    Wu, H.H.3    Feigon, J.4
  • 35
    • 84988057355 scopus 로고
    • Oxidation of β-hydroxyketones and esters-a convenient synthesis of 1,3-diketones and β-ketoesters
    • Smith A.B., and Levenberg P.A. Oxidation of β-hydroxyketones and esters-a convenient synthesis of 1,3-diketones and β-ketoesters. Synthesis (1981) 567-570
    • (1981) Synthesis , pp. 567-570
    • Smith, A.B.1    Levenberg, P.A.2
  • 38
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas J., Ouyang Z., Tseng J., Binkowski A., Turpaz Y., and Liang J. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 34 (2006) W116-W118
    • (2006) Nucleic Acids Res. , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 39
    • 0142135988 scopus 로고    scopus 로고
    • Polyketide chain length control by chain length factor
    • Tang Y., Tsai S.C., and Khosla C. Polyketide chain length control by chain length factor. J. Am. Chem. Soc. 125 (2003) 12708-12709
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12708-12709
    • Tang, Y.1    Tsai, S.C.2    Khosla, C.3
  • 40
    • 0032562124 scopus 로고    scopus 로고
    • Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase
    • Carreras C.W., and Khosla C. Purification and in vitro reconstitution of the essential protein components of an aromatic polyketide synthase. Biochemistry 37 (1998) 2084-2088
    • (1998) Biochemistry , vol.37 , pp. 2084-2088
    • Carreras, C.W.1    Khosla, C.2
  • 41
    • 0031931702 scopus 로고    scopus 로고
    • Catalytic self-acylation of type II polyketide synthase acyl carrier proteins
    • Hitchman T.S., Crosby J., Byrom K.J., Cox R.J., and Simpson T.J. Catalytic self-acylation of type II polyketide synthase acyl carrier proteins. Chem. Biol. 5 (1998) 35-47
    • (1998) Chem. Biol. , vol.5 , pp. 35-47
    • Hitchman, T.S.1    Crosby, J.2    Byrom, K.J.3    Cox, R.J.4    Simpson, T.J.5
  • 42
    • 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. 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 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 43
    • 0029064652 scopus 로고
    • Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits
    • McDaniel R., Ebert-Khosla S., Hopwood D.A., and Khosla C. Rational design of aromatic polyketide natural products by recombinant assembly of enzymatic subunits. Nature 375 (1995) 549-554
    • (1995) Nature , vol.375 , pp. 549-554
    • McDaniel, R.1    Ebert-Khosla, S.2    Hopwood, D.A.3    Khosla, C.4
  • 44
    • 39649122833 scopus 로고    scopus 로고
    • Inhibition kinetics and emodin co-crystal structure of a type II polyketide ketoreductase
    • Korman T.P., Tan Y.H., Wong J., Luo R., and Tsai S.C. Inhibition kinetics and emodin co-crystal structure of a type II polyketide ketoreductase. Biochemistry 47 (2008) 1837-1847
    • (2008) Biochemistry , vol.47 , pp. 1837-1847
    • Korman, T.P.1    Tan, Y.H.2    Wong, J.3    Luo, R.4    Tsai, S.C.5
  • 46
    • 0032529079 scopus 로고    scopus 로고
    • Concentration and desalting of protein samples for mass spectrometry analysis
    • Winston R.L., and Fitzgerald M.C. Concentration and desalting of protein samples for mass spectrometry analysis. Anal. Biochem. 262 (1998) 83-85
    • (1998) Anal. Biochem. , vol.262 , pp. 83-85
    • Winston, R.L.1    Fitzgerald, M.C.2
  • 47
    • 0029085632 scopus 로고
    • Polyketide synthase acyl carrier proteins from Streptomyces-expression in Escherichia coli, purification and partial characterization
    • Crosby J., Sherman D.H., Bibb M.J., Revill W.P., Hopwood D.A., and Simpson T.J. Polyketide synthase acyl carrier proteins from Streptomyces-expression in Escherichia coli, purification and partial characterization. Biochim. Biophys. Acta 1251 (1995) 32-42
    • (1995) Biochim. Biophys. Acta , vol.1251 , pp. 32-42
    • Crosby, J.1    Sherman, D.H.2    Bibb, M.J.3    Revill, W.P.4    Hopwood, D.A.5    Simpson, T.J.6
  • 52
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: development of a software pipeline
    • Vranken W.F., Boucher W., Stevens T.J., Fogh R.H., Pajon A., Llinas M., et al. The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59 (2005) 687-696
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Stevens, T.J.3    Fogh, R.H.4    Pajon, A.5    Llinas, M.6
  • 54
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • Nilges M., Macias M.J., O'Donoghue S.I., and Oschkinat H. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin. J. Mol. Biol. 269 (1997) 408-422
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 55
    • 2442561255 scopus 로고    scopus 로고
    • Correction of spin diffusion during iterative automated NOE assignment
    • Linge J.P., Habeck M., Rieping W., and Nilges M. Correction of spin diffusion during iterative automated NOE assignment. J. Magn. Reson. 167 (2004) 334-342
    • (2004) J. Magn. Reson. , vol.167 , pp. 334-342
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 56
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 58
    • 19944407188 scopus 로고    scopus 로고
    • Quantitative study of the effects of chemical shift tolerances and rates of SA cooling on structure calculation from automatically assigned NOE data
    • Fossi M., Oschkinat H., Nilges M., and Ball L.J. Quantitative study of the effects of chemical shift tolerances and rates of SA cooling on structure calculation from automatically assigned NOE data. J. Magn. Reson. 175 (2005) 92-102
    • (2005) J. Magn. Reson. , vol.175 , pp. 92-102
    • Fossi, M.1    Oschkinat, H.2    Nilges, M.3    Ball, L.J.4
  • 60


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.