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Volumn 45, Issue 22, 2006, Pages 6904-6916

Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; PHASE EQUILIBRIA; POLYPEPTIDES; SOLUTIONS; THREE DIMENSIONAL;

EID: 33744954170     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060368u     Document Type: Article
Times cited : (63)

References (60)
  • 2
    • 0142196023 scopus 로고    scopus 로고
    • Drug resistance in parasites: Can we stay ahead of the evolutionary curve?
    • Sibley, C. H., and Hunt, S. Y. (2003) Drug resistance in parasites: can we stay ahead of the evolutionary curve? Trends Parasitol. 19, 532-537.
    • (2003) Trends Parasitol. , vol.19 , pp. 532-537
    • Sibley, C.H.1    Hunt, S.Y.2
  • 3
    • 2142659388 scopus 로고    scopus 로고
    • Antimalarial drug resistance
    • White, N. J. (2004) Antimalarial drug resistance, J. Clin. Invest. 113, 1084-1092.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1084-1092
    • White, N.J.1
  • 4
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia, N., and Surolia, A. (2001) Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum, Nat. Med. 7, 167-173.
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 6
    • 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. (2005) The structural biology of type II fatty acid biosynthesis, Annu. Rev. Biochem. 74, 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
  • 8
    • 0034780806 scopus 로고    scopus 로고
    • Bacterial fatty acid biosynthesis: Targets for antibacterial drug discovery
    • Campbell, J. W., and Cronan, J. E., Jr. (2001) Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery, Annu. Rev. Microbiol. 55, 305-332.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 305-332
    • Campbell, J.W.1    Cronan Jr., J.E.2
  • 9
    • 0023813070 scopus 로고
    • Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations
    • Holak, T. A., Kearsley, S. K., Kim, Y., and Prestegard, J. H. (1988) Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations, Biochemistry 27, 6135-6142.
    • (1988) Biochemistry , vol.27 , pp. 6135-6142
    • Holak, T.A.1    Kearsley, S.K.2    Kim, Y.3    Prestegard, J.H.4
  • 10
    • 0023677654 scopus 로고
    • Three-dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry
    • Holak, T. A., Nilges, M., Prestegard, J. H., Gronenborn, A. M., and Clore, G. M. (1988) Three-dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry, Eur. J. Biochem. 175 (1), 9-15.
    • (1988) Eur. J. Biochem. , vol.175 , Issue.1 , pp. 9-15
    • Holak, T.A.1    Nilges, M.2    Prestegard, J.H.3    Gronenborn, A.M.4    Clore, G.M.5
  • 11
    • 0024559147 scopus 로고
    • Improved strategies for the determination of protein structures from NMR data: The solution structure of acyl carrier protein
    • Holak, T. A., Nilges, M., and Oschkinat, H. (1989) Improved strategies for the determination of protein structures from NMR data: the solution structure of acyl carrier protein, FEBS Lett. 242, 218-224.
    • (1989) FEBS Lett. , vol.242 , pp. 218-224
    • Holak, T.A.1    Nilges, M.2    Oschkinat, H.3
  • 12
    • 0025613125 scopus 로고
    • Refinement of the NMR structures for acyl carrier protein with scalar coupling data
    • Kim, Y., and Prestegard, J. H. (1990) Refinement of the NMR structures for acyl carrier protein with scalar coupling data, Proteins (3rd Ed.) 8, 377-385.
    • (1990) Proteins (3rd Ed.) , vol.8 , pp. 377-385
    • Kim, Y.1    Prestegard, J.H.2
  • 13
    • 0034886054 scopus 로고    scopus 로고
    • Solution structure of B. subtilis acyl carrier protein
    • Xu, G.-Y., Tam, A., Lin, L., Hixon, J., Fritz, C. C., and Powers, R. (2001) Solution structure of B. subtilis acyl carrier protein, Structure 9, 277-287.
    • (2001) Structure , vol.9 , pp. 277-287
    • Xu, G.-Y.1    Tam, A.2    Lin, L.3    Hixon, J.4    Fritz, C.C.5    Powers, R.6
  • 14
    • 0037013187 scopus 로고    scopus 로고
    • The solution structure of acyl carrier protein from Mycobacterium tuberculosis
    • Wong, H. C., Liu, G., Zhang, Y.-M., Rock, C. O., and Zheng, J. (2002) The solution structure of acyl carrier protein from Mycobacterium tuberculosis, J. Biol. Chem. 277, 15874-15880.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15874-15880
    • Wong, H.C.1    Liu, G.2    Zhang, Y.-M.3    Rock, C.O.4    Zheng, J.5
  • 16
    • 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. (1997) Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2), Biochemistry 36, 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
  • 17
    • 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. (2003) Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein, Biochemistry 42, 4648-4657.
    • (2003) Biochemistry , vol.42 , pp. 4648-4657
    • Li, Q.1    Khosla, C.2    Puglisi, J.D.3    Liu, C.W.4
  • 18
    • 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. (2003) Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus, Biochemistry 42, 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
  • 19
    • 16644400323 scopus 로고    scopus 로고
    • Structure of apo acyl carrier protein and a proposal to engineer protein crystallization through metal ions
    • Qiu, X., and Janson, C. A. (2004) Structure of apo acyl carrier protein and a proposal to engineer protein crystallization through metal ions, Acta Crystallogr., Sect. D 60, 1545-1554.
    • (2004) Acta Crystallogr., Sect. D , vol.60 , pp. 1545-1554
    • Qiu, X.1    Janson, C.A.2
  • 20
  • 21
    • 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. (2000) 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. Folding Des. 8, 883-895.
    • (2000) Struct. Folding 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
  • 22
    • 0037238269 scopus 로고    scopus 로고
    • The application of computational methods to explore the diversity and structure of bacterial fatty acid synthase
    • Zhang, Y. M., Marrakchi, H., White, S. W., and Rock, C. O. (2003) The application of computational methods to explore the diversity and structure of bacterial fatty acid synthase, J. Lipid Res. 44, 1-10
    • (2003) J. Lipid Res. , vol.44 , pp. 1-10
    • Zhang, Y.M.1    Marrakchi, H.2    White, S.W.3    Rock, C.O.4
  • 23
    • 0024435205 scopus 로고
    • A dynamic model for the structure of acyl carrier protein in solution
    • Kim, Y., and Prestegard, J. H. (1989) A dynamic model for the structure of acyl carrier protein in solution, Biochemistry 28, 8792-8797.
    • (1989) Biochemistry , vol.28 , pp. 8792-8797
    • Kim, Y.1    Prestegard, J.H.2
  • 24
    • 0025087892 scopus 로고
    • Demonstration of a conformational equilibrium in acyl carrier protein from spinach using rotating frame nuclear magnetic resonance spectroscopy
    • Kim, Y., and Prestegard, J. H. (1990) Demonstration of a conformational equilibrium in acyl carrier protein from spinach using rotating frame nuclear magnetic resonance spectroscopy, J. Am. Chem. Soc. 112, 3707-3709.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3707-3709
    • Kim, Y.1    Prestegard, J.H.2
  • 25
    • 17044372337 scopus 로고    scopus 로고
    • A novel approach for overexpression, characterization, and isotopic enrichment of a homogeneous species of acyl carrier protein from Plasmodium falciparum
    • Sharma, S. K., Modak, R., Sharma, S., Sharma, A. K., Sarma, S. P., Surolia, A., and Surolia, N. (2005) A novel approach for overexpression, characterization, and isotopic enrichment of a homogeneous species of acyl carrier protein from Plasmodium falciparum, Biochem. Biophys. Res. Commun. 330, 1019-1026.
    • (2005) Biochem. Biophys. Res. Commun. , vol.330 , pp. 1019-1026
    • Sharma, S.K.1    Modak, R.2    Sharma, S.3    Sharma, A.K.4    Sarma, S.P.5    Surolia, A.6    Surolia, N.7
  • 26
    • 0025193295 scopus 로고
    • 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins
    • 13C for assignment and interpretation of nuclear magnetic resonance spectra of proteins, Q. Rev. Biophys. 23, 1-38.
    • (1990) Q. Rev. Biophys. , vol.23 , pp. 1-38
    • McIntosh, L.P.1    Dahlquist, F.W.2
  • 27
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion, D., Ikura, M., Tschudin, R., and Bax, A. (1989) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins, J. Magn. Reson. 85, 393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 28
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 29
    • 0001250026 scopus 로고
    • ANSIG: A program for the assignment of protein 1H 2D NMR spectra by interactive graphics
    • Kraulis, P. J. (1989) ANSIG: a program for the assignment of protein 1H 2D NMR spectra by interactive graphics, J. Magn. Reson. 84, 627-633.
    • (1989) J. Magn. Reson. , vol.84 , pp. 627-633
    • Kraulis, P.J.1
  • 30
    • 0028204451 scopus 로고
    • Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • Kraulis, P. J., Domaille, P. J., Campbell-Burk, S. L., Van Aken, T., and Laue, E. D. (1994) Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy, Biochemistry 33 (12), 3515-3531.
    • (1994) Biochemistry , vol.33 , Issue.12 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 32
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax, A., and Grzesiek, S. (1993) Methodological advances in protein NMR, Acc. Chem. Res. 26, 131-138.
    • (1993) Acc. Chem. Res. , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 37
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and Szabo, A. (1982a) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 38
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • Lipari, G., and Szabo, A. (1982b) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results, J. Am. Chem. Soc. 104, 4559-4570.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 39
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli Ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G. (1995) Backbone dynamics of Escherichia coli Ribonuclease HI: correlations with structure and function in an active enzyme, J. Mol. Biol. 246, 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 40
    • 12044256620 scopus 로고
    • Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy
    • Palmer, A. G., Rance, M., and Wright, P. E. (1991) Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy, J. Am. Chem. Soc. 113, 4371-4380.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4371-4380
    • Palmer, A.G.1    Rance, M.2    Wright, P.E.3
  • 41
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA, J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 42
    • 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. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 43
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR, J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 44
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R. B., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-5, 29-32.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.B.1    Billeter, M.2    Wüthrich, K.3
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins: Struct., Funct., Genet. 11, 281-296.
    • (1991) Proteins: Struct., Funct., Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 47
    • 0023989064 scopus 로고
    • Improved tools for the biological sequence comparison
    • Pearson, W. R., and Lipman, D. J. (1988) Improved tools for the biological sequence comparison, Proc. Natl. Acad. Sci. U.S.A. 85, 2444-2448.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 48
    • 24344473350 scopus 로고    scopus 로고
    • NMR assignment of the holo-ACP from malaria parasite Plasmodium falciparum
    • Sharma, A. K., Sharma, S. K., Surolia, N., and Sarma, S. P. (2005) NMR assignment of the holo-ACP from malaria parasite Plasmodium falciparum, J. Biomol. NMR 32, 260.
    • (2005) J. Biomol. NMR , vol.32 , pp. 260
    • Sharma, A.K.1    Sharma, S.K.2    Surolia, N.3    Sarma, S.P.4
  • 49
    • 0028393784 scopus 로고
    • The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data
    • Wishart, D. S., and Sykes, B. D. (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data, J. Biomol. NMR 4, 171-180.
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 50
    • 0035838447 scopus 로고    scopus 로고
    • Biosynthesis of D-alanyl-lipoteichoic acid: The tertiary structure of apo-D-alanyl carrier protein
    • Volkman, B. F., Zhang, Q., Debabov, D. V., Rivera, E., Kresheck, G. C., and Neuhaus, F. C. (2001) Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein, Biochemistry 40, 7964-7972.
    • (2001) Biochemistry , vol.40 , pp. 7964-7972
    • Volkman, B.F.1    Zhang, Q.2    Debabov, D.V.3    Rivera, E.4    Kresheck, G.C.5    Neuhaus, F.C.6
  • 51
  • 52
    • 0034916655 scopus 로고    scopus 로고
    • Magnetic relaxation dispersion studies of biomolecular solutions
    • Halle, B., and Denisov, V. P. (2001) Magnetic relaxation dispersion studies of biomolecular solutions, Methods Enzymol. 338, 178-201.
    • (2001) Methods Enzymol. , vol.338 , pp. 178-201
    • Halle, B.1    Denisov, V.P.2
  • 53
    • 0031984752 scopus 로고    scopus 로고
    • Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain
    • Akke, M., Liu, J., Cavanagh, J., Erickson, H. P., and Palmer, A. G., III. (1998) Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain, Nat. Struct. Biol. 5, 55-59.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 55-59
    • Akke, M.1    Liu, J.2    Cavanagh, J.3    Erickson, H.P.4    Palmer III, A.G.5
  • 55
    • 0030936547 scopus 로고    scopus 로고
    • Ability of Streptomyces supp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E. coli holo-ACP synthase
    • Gehring, A. M., Lambalot, R. H., Vogel, K. W., Drueckhammer, D. G., and Walsh, C. T. (1997) Ability of Streptomyces supp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E.coli holo-ACP synthase, Chem. Biol. 4, 17-24.
    • (1997) Chem. Biol. , vol.4 , pp. 17-24
    • Gehring, A.M.1    Lambalot, R.H.2    Vogel, K.W.3    Drueckhammer, D.G.4    Walsh, C.T.5
  • 56
    • 0037417775 scopus 로고    scopus 로고
    • The initiating steps of a type II fatty acid synthase in Plasmodium falciparum are catalyzed by pfACP, pfMCAT, and pfKASIII
    • Prigge, S. T. He, X. Gerena, L., Waters, N. C., and Reynolds, K. A. (2003) The initiating steps of a type II fatty acid synthase in Plasmodium falciparum are catalyzed by pfACP, pfMCAT, and pfKASIII, Biochemistry 42, 1160-1169.
    • (2003) Biochemistry , vol.42 , pp. 1160-1169
    • Prigge, S.T.1    He, X.2    Gerena, L.3    Waters, N.C.4    Reynolds, K.A.5
  • 58
    • 0022296924 scopus 로고
    • Acyl carrier protein from Escherichia coli. Structural characterization of short-chain acylated acyl carrier proteins by NMR
    • Mayo, K. H., and Prestegard, J. H. (1985) Acyl carrier protein from Escherichia coli. Structural characterization of short-chain acylated acyl carrier proteins by NMR, Biochemistry 24, 7834-7838.
    • (1985) Biochemistry , vol.24 , pp. 7834-7838
    • Mayo, K.H.1    Prestegard, J.H.2
  • 59
    • 0023645162 scopus 로고
    • 1H Heteronuclear nuclear overhauser effect studies of the acyl chain-binding site of acyl carrier protein
    • 1H Heteronuclear nuclear overhauser effect studies of the acyl chain-binding site of acyl carrier protein, J. Biol. Chem. 262, 8963-8965.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8963-8965
    • Jones, P.-J.1    Cioffi, E.A.2    Prestegard, J.H.3
  • 60
    • 0032033207 scopus 로고    scopus 로고
    • Heterologously expressed acyl carrier protein domain of rat fatty acid synthase functions in Escherichia coli fatty acid synthase and Streptomyces coelicolor polyketide synthase systems
    • Tropf, S., Revill, W. P., Bibb, M. J., Hopwood, D. A., and Schweizer, M. (1998) Heterologously expressed acyl carrier protein domain of rat fatty acid synthase functions in Escherichia coli fatty acid synthase and Streptomyces coelicolor polyketide synthase systems, Chem. Biol. 5, 135-146.
    • (1998) Chem. Biol. , vol.5 , pp. 135-146
    • Tropf, S.1    Revill, W.P.2    Bibb, M.J.3    Hopwood, D.A.4    Schweizer, M.5


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