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Volumn 365, Issue 1, 2007, Pages 135-145

Structural Studies of Fatty Acyl-(Acyl Carrier Protein) Thioesters Reveal a Hydrophobic Binding Cavity that Can Expand to Fit Longer Substrates

Author keywords

acyl carrier protein; acyl chain binding; conformational changes; fatty acid biosynthesis; hydrophobic binding pocket

Indexed keywords

ACYL CARRIER PROTEIN; FATTY ACID; PANTETHEINE PHOSPHATE; SERINE;

EID: 33751512907     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.09.049     Document Type: Article
Times cited : (138)

References (41)
  • 2
    • 0026861825 scopus 로고
    • The biochemistry and molecular-biology of plant lipid biosynthesis
    • Slabas A.R., and Fawcett T. The biochemistry and molecular-biology of plant lipid biosynthesis. Plant Mol. Biol. 19 (1992) 169-191
    • (1992) Plant Mol. Biol. , vol.19 , pp. 169-191
    • Slabas, A.R.1    Fawcett, T.2
  • 3
    • 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-Lipids Lipid Metab. 1302 (1996) 1-16
    • (1996) Biochim. Biophys. Acta-Lipids Lipid Metab. , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan, J.E.2
  • 4
    • 10944262320 scopus 로고    scopus 로고
    • Acyl carrier protein is a cellular target for the antibacterial action of the pantothenamide class of pantothenate antimetabolites
    • Zhang Y.M., Frank M.W., Virga K.G., Lee R.E., Rock C.O., and Jackowski S. Acyl carrier protein is a cellular target for the antibacterial action of the pantothenamide class of pantothenate antimetabolites. J. Biol. Chem. 279 (2004) 50969-50975
    • (2004) J. Biol. Chem. , vol.279 , pp. 50969-50975
    • Zhang, Y.M.1    Frank, M.W.2    Virga, K.G.3    Lee, R.E.4    Rock, C.O.5    Jackowski, S.6
  • 5
    • 0026747889 scopus 로고
    • Purification and characterization of the acyl carrier protein of the Streptomyces glaucescens Tetracenomycin C polyketide synthase
    • Shen B., Summers R.G., Gramajo H., Bibb M.J., and Hutchinson C.R. Purification and characterization of the acyl carrier protein of the Streptomyces glaucescens Tetracenomycin C polyketide synthase. J. Bacteriol. 174 (1992) 3818-3821
    • (1992) J. Bacteriol. , vol.174 , pp. 3818-3821
    • Shen, B.1    Summers, R.G.2    Gramajo, H.3    Bibb, M.J.4    Hutchinson, C.R.5
  • 6
    • 0029730638 scopus 로고    scopus 로고
    • A special acyl carrier protein for transferring long hydroxylated fatty acids to lipid a in Rhizobium
    • Brozek K.A., Carlson R.W., and Raetz C.R.H. A special acyl carrier protein for transferring long hydroxylated fatty acids to lipid a in Rhizobium. J. Biol. Chem. 271 (1996) 32126-32136
    • (1996) J. Biol. Chem. , vol.271 , pp. 32126-32136
    • Brozek, K.A.1    Carlson, R.W.2    Raetz, C.R.H.3
  • 8
    • 0025731587 scopus 로고
    • Isolation of the Rhizobium leguminosarum Nodf nodulation protein - Nodf carries a 4′-phosphopantetheine prosthetic group
    • Geiger O., Spaink H.P., and Kennedy E.P. Isolation of the Rhizobium leguminosarum Nodf nodulation protein - Nodf carries a 4′-phosphopantetheine prosthetic group. J. Bacteriol. 173 (1991) 2872-2878
    • (1991) J. Bacteriol. , vol.173 , pp. 2872-2878
    • Geiger, O.1    Spaink, H.P.2    Kennedy, E.P.3
  • 9
    • 0022524388 scopus 로고
    • An essential function for acyl carrier protein in the biosynthesis of membrane-derived oligosaccharides of Escherichia coli
    • Therisod H., Weissborn A.C., and Kennedy E.P. An essential function for acyl carrier protein in the biosynthesis of membrane-derived oligosaccharides of Escherichia coli. Proc. Natl Acad. Sci. USA 83 (1986) 7236-7240
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 7236-7240
    • Therisod, H.1    Weissborn, A.C.2    Kennedy, E.P.3
  • 10
    • 0029817781 scopus 로고    scopus 로고
    • Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fescheri LuxI protein
    • Schaefer A.L., Val D.L., Hanzelka B.L., Cronan J.E., and Greenberg E.P. Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fescheri LuxI protein. Proc. Natl Acad. Sci. USA 93 (1996) 9505-9509
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 9505-9509
    • Schaefer, A.L.1    Val, D.L.2    Hanzelka, B.L.3    Cronan, J.E.4    Greenberg, E.P.5
  • 11
    • 0022410208 scopus 로고
    • Acyl-acyl carrier protein as a source of fatty-acids for bacterial bioluminescence
    • Byers D.M., and Meighen E.A. Acyl-acyl carrier protein as a source of fatty-acids for bacterial bioluminescence. Proc. Natl Acad. Sci. USA 82 (1985) 6085-6089
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 6085-6089
    • Byers, D.M.1    Meighen, E.A.2
  • 12
    • 0020673858 scopus 로고
    • Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts
    • Frentzen M., Heinz E., McKeon T.A., and Stumpf P.K. Specificities and selectivities of glycerol-3-phosphate acyltransferase and monoacylglycerol-3-phosphate acyltransferase from pea and spinach chloroplasts. Eur. J. Biochem. 129 (1983) 629-636
    • (1983) Eur. J. Biochem. , vol.129 , pp. 629-636
    • Frentzen, M.1    Heinz, E.2    McKeon, T.A.3    Stumpf, P.K.4
  • 13
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel J.P., Koronakis V., and Hughes C. Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature 351 (1991) 759-761
    • (1991) Nature , vol.351 , pp. 759-761
    • Issartel, J.P.1    Koronakis, V.2    Hughes, C.3
  • 14
    • 0030747906 scopus 로고    scopus 로고
    • A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria
    • Jordan S.W., and Cronan J.E. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272 (1997) 17903-17906
    • (1997) J. Biol. Chem. , vol.272 , pp. 17903-17906
    • Jordan, S.W.1    Cronan, J.E.2
  • 15
    • 1942488270 scopus 로고    scopus 로고
    • pH-induced conformational transition of H.pylori acyl carrier protein: insight into the unfolding of local structure
    • Park S.J., Kim J.S., Son W.S., and Lee B.J. pH-induced conformational transition of H.pylori acyl carrier protein: insight into the unfolding of local structure. J. Biochem. 135 (2004) 337-346
    • (2004) J. Biochem. , vol.135 , pp. 337-346
    • Park, S.J.1    Kim, J.S.2    Son, W.S.3    Lee, B.J.4
  • 16
    • 0025613125 scopus 로고
    • Refinement of the NMR structures for acyl carrier protein with scalar coupling data
    • Kim Y.M., and Prestegard J.H. Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins: Struct. Funct. Genet. 8 (1990) 377-385
    • (1990) Proteins: Struct. Funct. Genet. , vol.8 , pp. 377-385
    • Kim, Y.M.1    Prestegard, J.H.2
  • 17
    • 0023677654 scopus 로고
    • 3-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. 3-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 (1988) 9-15
    • (1988) Eur. J. Biochem. , vol.175 , pp. 9-15
    • Holak, T.A.1    Nilges, M.2    Prestegard, J.H.3    Gronenborn, A.M.4    Clore, G.M.5
  • 18
    • 0023813070 scopus 로고
    • 3-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. 3-Dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations. Biochemistry 27 (1988) 6135-6142
    • (1988) Biochemistry , vol.27 , pp. 6135-6142
    • Holak, T.A.1    Kearsley, S.K.2    Kim, Y.3    Prestegard, J.H.4
  • 19
    • 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. Improved strategies for the determination of protein structures from NMR data. The solution structure of acyl carrier protein. FEBS Letters 242 (1989) 218-224
    • (1989) FEBS Letters , vol.242 , pp. 218-224
    • Holak, T.A.1    Nilges, M.2    Oschkinat, H.3
  • 20
    • 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., et al. 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. Design 8 (2000) 883-895
    • (2000) Struct. Fold. Design , vol.8 , pp. 883-895
    • Parris, K.D.1    Lin, L.2    Tam, A.3    Mathew, R.4    Hixon, J.5    Stahl, M.6
  • 21
  • 22
    • 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
  • 23
    • 0037013187 scopus 로고    scopus 로고
    • The solution structure of acyl carrier protein from Mycobacterium tuberculosis
    • Wong H.C., Liu G.H., Zhang Y.M., Rock C.O., and Zheng J. The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 277 (2002) 15874-15880
    • (2002) J. Biol. Chem. , vol.277 , pp. 15874-15880
    • Wong, H.C.1    Liu, G.H.2    Zhang, Y.M.3    Rock, C.O.4    Zheng, J.5
  • 24
    • 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
  • 25
    • 0018787395 scopus 로고
    • Re-evaluation of the solution structure of acyl carrier protein
    • Rock C.O., and Cronan J.E. Re-evaluation of the solution structure of acyl carrier protein. J. Biol. Chem. 254 (1979) 9778-9785
    • (1979) J. Biol. Chem. , vol.254 , pp. 9778-9785
    • Rock, C.O.1    Cronan, J.E.2
  • 26
    • 0018787017 scopus 로고
    • Preparative enzymatic synthesis and hydrophobic chromatography of acyl-acyl carrier protein
    • Rock C.O., and Garwin J.L. Preparative enzymatic synthesis and hydrophobic chromatography of acyl-acyl carrier protein. J. Biol. Chem. 254 (1979) 7123-7128
    • (1979) J. Biol. Chem. , vol.254 , pp. 7123-7128
    • Rock, C.O.1    Garwin, J.L.2
  • 27
    • 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. Acyl carrier protein from Escherichia coli. Structural characterization of short chain acylated acyl carrier proteins by NMR. Biochemistry 24 (1985) 7834-7838
    • (1985) Biochemistry , vol.24 , pp. 7834-7838
    • Mayo, K.H.1    Prestegard, J.H.2
  • 28
    • 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 (1987) 8963-8965
    • (1987) J. Biol. Chem. , vol.262 , pp. 8963-8965
    • Jones, P.J.1    Cioffi, E.A.2    Prestegard, J.H.3
  • 29
    • 0036008524 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies on acyl-(acyl carrier protein) from Escherichia coli
    • Roujeinikova A., Baldock C., Simon W.J., Gilroy J., Baker P.J., Stuitje A.R., et al. Crystallization and preliminary X-ray crystallographic studies on acyl-(acyl carrier protein) from Escherichia coli. Acta Crystallog. sect. D 58 (2002) 330-332
    • (2002) Acta Crystallog. sect. D , vol.58 , pp. 330-332
    • Roujeinikova, A.1    Baldock, C.2    Simon, W.J.3    Gilroy, J.4    Baker, P.J.5    Stuitje, A.R.6
  • 30
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design
    • Liang J., Edelsbrunner H., and Woodward C. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein Sci. 7 (1998) 1884-1897
    • (1998) Protein Sci. , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3
  • 31
    • 0020804427 scopus 로고
    • Environment of the aromatic chromophores of acyl carrier protein
    • Rock C.O. Environment of the aromatic chromophores of acyl carrier protein. Arch. Biochem. Biophys. 225 (1983) 122-129
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 122-129
    • Rock, C.O.1
  • 32
    • 0346101746 scopus 로고    scopus 로고
    • Key residues responsible for acyl carrier protein and beta- ketoacyl-acyl carrier protein reductase (FabG) interaction
    • Zhang Y.M., Wu B.N., Zheng J., and Rock C.O. Key residues responsible for acyl carrier protein and beta- ketoacyl-acyl carrier protein reductase (FabG) interaction. J. Biol. Chem. 278 (2003) 52935-52943
    • (2003) J. Biol. Chem. , vol.278 , pp. 52935-52943
    • Zhang, Y.M.1    Wu, B.N.2    Zheng, J.3    Rock, C.O.4
  • 33
    • 0037435617 scopus 로고    scopus 로고
    • Amino acid residues of Escherichia coli acyl carrier protein involved in heterologous protein interactions
    • Worsham L.A.S., Earls L., Jolly C., Langston K.G., Trent M.S., and Ernst-Fonberg M.L. Amino acid residues of Escherichia coli acyl carrier protein involved in heterologous protein interactions. Biochemistry 42 (2003) 167-176
    • (2003) Biochemistry , vol.42 , pp. 167-176
    • Worsham, L.A.S.1    Earls, L.2    Jolly, C.3    Langston, K.G.4    Trent, M.S.5    Ernst-Fonberg, M.L.6
  • 34
    • 0035929665 scopus 로고    scopus 로고
    • Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity
    • Flaman A.S., Chen J.M., Van Iderstine S.C., and Byers D.M. Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity. J. Biol. Chem. 276 (2001) 35934-35939
    • (2001) J. Biol. Chem. , vol.276 , pp. 35934-35939
    • Flaman, A.S.1    Chen, J.M.2    Van Iderstine, S.C.3    Byers, D.M.4
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 39
    • 0000243829 scopus 로고
    • Procheck - a program to check the stereochemical quality of protein structures
    • Laskowski R.A., Macarthur M.W., Moss D.S., and Thornton J.M. Procheck - a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A 42 (1986) 140-149
    • (1986) Acta Crystallog. sect. A , vol.42 , pp. 140-149
    • Read, R.J.1


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