메뉴 건너뛰기




Volumn 8, Issue 2, 2000, Pages 185-195

The 1.8 Å crystal structure and active-site architecture of β- ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli

Author keywords

Acyl carrier protein; Coenzyme A; Condensing enzymes; Crystal structure; Fatty acids

Indexed keywords

3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE; FATTY ACID SYNTHASE; 3 KETOACYL ACYL CARRIER PROTEIN SYNTHASE III; 3-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III; PRIMER DNA;

EID: 0034651317     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00094-0     Document Type: Article
Times cited : (219)

References (49)
  • 1
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock C.O., Cronan J.E. Jr. 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., Jr.2
  • 2
    • 0342972699 scopus 로고
    • Fatty acid synthetase: Plants and bacteria have similar organization
    • Ohlrogge J.B. Fatty acid synthetase: plants and bacteria have similar organization. TIBS. 7:1982;386-387.
    • (1982) TIBS , vol.7 , pp. 386-387
    • Ohlrogge, J.B.1
  • 3
    • 0028156861 scopus 로고
    • InhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis
    • Banerjee A., Jacobs W.R. Jr.et al. inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science. 263:1994;227-230.
    • (1994) Science , vol.263 , pp. 227-230
    • Banerjee, A.1    Jacobs W.R., Jr.2
  • 4
    • 0032490937 scopus 로고    scopus 로고
    • Triclosan targets lipid synthesis
    • McMurray L.M., Oethinger M., Levy S. Triclosan targets lipid synthesis. Nature. 394:1998;531-532.
    • (1998) Nature , vol.394 , pp. 531-532
    • McMurray, L.M.1    Oethinger, M.2    Levy, S.3
  • 5
    • 0032515066 scopus 로고    scopus 로고
    • Broad spectrum antimicrobial biocides target the FabI component of fatty acid synthesis
    • Heath R.J., Yu Y.-T., Shapiro M.A., Olson E., Rock C.O. Broad spectrum antimicrobial biocides target the FabI component of fatty acid synthesis. J. Biol. Chem. 273:1998;30316-30321.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30316-30321
    • Heath, R.J.1    Yu, Y.-T.2    Shapiro, M.A.3    Olson, E.4    Rock, C.O.5
  • 6
    • 0029257316 scopus 로고
    • Modification of Brassica napus seed oil by expression of the Escherichia coli fabH gene, encoding 3-ketoacyl-acyl carrier protein synthase III
    • Verwoert II G.S., van der Linden K.H., Walsh M.C., Nijkamp H.J.J., Stuitje A.R. Modification of Brassica napus seed oil by expression of the Escherichia coli fabH gene, encoding 3-ketoacyl-acyl carrier protein synthase III. Plant Mol. Biol. 27:1995;875-886.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 875-886
    • Verwoert G.S. II1    Van Der Linden, K.H.2    Walsh, M.C.3    Nijkamp, H.J.J.4    Stuitje, A.R.5
  • 7
    • 0344549379 scopus 로고    scopus 로고
    • Nuclear-endcoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum
    • Waller R.F., McFadden G.I.et al. Nuclear-endcoded proteins target to the plastid in Toxoplasma gondii and Plasmodium falciparum. Proc. Natl Acad. Sci. USA. 95:1998;12352-12357.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12352-12357
    • Waller, R.F.1    McFadden, G.I.2
  • 8
    • 0026415106 scopus 로고
    • Modular organization of genes required for complex polyketide biosynthesis
    • Donadio S., Staver M.J., McAlpine J.B., Swanson S.J., Katz L. Modular organization of genes required for complex polyketide biosynthesis. Science. 252:1991;675-679.
    • (1991) Science , vol.252 , pp. 675-679
    • Donadio, S.1    Staver, M.J.2    McAlpine, J.B.3    Swanson, S.J.4    Katz, L.5
  • 9
    • 0029440560 scopus 로고
    • Genetics of antibiotic production in Streptomyces coelicolor A3(2), a model streptomycete
    • Hopwood D.A., Chater K.F., Bibb M.J. Genetics of antibiotic production in Streptomyces coelicolor A3(2), a model streptomycete. Biotechnology. 28:1995;65-102.
    • (1995) Biotechnology , vol.28 , pp. 65-102
    • Hopwood, D.A.1    Chater, K.F.2    Bibb, M.J.3
  • 10
    • 0027742458 scopus 로고
    • Structure, function and regulation of chalcone synthase
    • Martin C.R. Structure, function and regulation of chalcone synthase. Int. Rev. Cytol. 147:1993;233-284.
    • (1993) Int. Rev. Cytol. , vol.147 , pp. 233-284
    • Martin, C.R.1
  • 11
    • 17544367317 scopus 로고    scopus 로고
    • Inhibition of β-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli
    • Heath R.J., Rock C.O. Inhibition of β-ketoacyl-acyl carrier protein synthase III (FabH) by acyl-acyl carrier protein in Escherichia coli. J. Biol. Chem. 271:1996;10996-11000.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10996-11000
    • Heath, R.J.1    Rock, C.O.2
  • 12
    • 0026775039 scopus 로고
    • Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12
    • Tsay J.-T., Oh W., Larson T.J., Jackowski S., Rock C.O. Isolation and characterization of the β-ketoacyl-acyl carrier protein synthase III gene (fabH) from Escherichia coli K-12. J. Biol. Chem. 267:1992;6807-6814.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6807-6814
    • Tsay, J.-T.1    Oh, W.2    Larson, T.J.3    Jackowski, S.4    Rock, C.O.5
  • 13
    • 0020351537 scopus 로고
    • Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo
    • Rock C.O., Jackowski S. Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo. J. Biol. Chem. 257:1982;10759-10765.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10759-10765
    • Rock, C.O.1    Jackowski, S.2
  • 14
    • 0028149560 scopus 로고
    • Alteration of the specificity and regulation of fatty acid synthesis of Escherichia coli by expression of a plant medium-chain acyl-acyl carrier protein thioesterase
    • Voelker T.A., Davies H.M. Alteration of the specificity and regulation of fatty acid synthesis of Escherichia coli by expression of a plant medium-chain acyl-acyl carrier protein thioesterase. J. Bacteriol. 176:1994;7320-7327.
    • (1994) J. Bacteriol. , vol.176 , pp. 7320-7327
    • Voelker, T.A.1    Davies, H.M.2
  • 15
    • 0028335691 scopus 로고
    • Inhibition of fatty acid synthesis in Escherichia coli in the absence of phospholipid synthesis and release of inhibition by thioesterase action
    • Jiang P., Cronan J.E. Jr. Inhibition of fatty acid synthesis in Escherichia coli in the absence of phospholipid synthesis and release of inhibition by thioesterase action. J. Bacteriol. 176:1994;2814-2821.
    • (1994) J. Bacteriol. , vol.176 , pp. 2814-2821
    • Jiang, P.1    Cronan J.E., Jr.2
  • 16
    • 0028960890 scopus 로고
    • Defective export of a periplasmic enzyme disrupts regulation of bacterial fatty acid synthesis
    • Cho H., Cronan J.E. Jr. Defective export of a periplasmic enzyme disrupts regulation of bacterial fatty acid synthesis. J. Biol. Chem. 270:1995;4216-4219.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4216-4219
    • Cho, H.1    Cronan J.E., Jr.2
  • 17
    • 0028032946 scopus 로고
    • Guanosine tetraphosphate inhibition of fatty acid and phospholipid synthesis in Escherichia coli is relieved by overexpression of glycerol-3-phosphate acyltransferase (plsB)
    • Heath R.J., Jackowski S., Rock C.O. Guanosine tetraphosphate inhibition of fatty acid and phospholipid synthesis in Escherichia coli is relieved by overexpression of glycerol-3-phosphate acyltransferase (plsB). J. Biol. Chem. 269:1994;26584-26590.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26584-26590
    • Heath, R.J.1    Jackowski, S.2    Rock, C.O.3
  • 18
    • 0030033704 scopus 로고    scopus 로고
    • Regulation of fatty acid elongation and initiation by acyl-acyl carrier protein in Escherichia coli
    • Heath R.J., Rock C.O. Regulation of fatty acid elongation and initiation by acyl-acyl carrier protein in Escherichia coli. J. Biol. Chem. 271:1996;1833-1836.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1833-1836
    • Heath, R.J.1    Rock, C.O.2
  • 19
    • 0032472224 scopus 로고    scopus 로고
    • Modification of NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis
    • Rozwarski D., Grant G., Barton D., Jacobs W., Sacchettini J.C. Modification of NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science. 279:1998;98-102.
    • (1998) Science , vol.279 , pp. 98-102
    • Rozwarski, D.1    Grant, G.2    Barton, D.3    Jacobs, W.4    Sacchettini, J.C.5
  • 21
    • 0024146365 scopus 로고
    • β-Ketoacyl-ACP synthase I of Escherichia coli: Nucleotide sequence of the fabB gene and identification of the cerulenin binding residue
    • Kauppinen S., Siggaard-Anderson M., van Wettstein-Knowles P. β-Ketoacyl-ACP synthase I of Escherichia coli: nucleotide sequence of the fabB gene and identification of the cerulenin binding residue. Carlsberg. Res. Commun. 53:1988;357-370.
    • (1988) Carlsberg. Res. Commun. , vol.53 , pp. 357-370
    • Kauppinen, S.1    Siggaard-Anderson, M.2    Van Wettstein-Knowles, P.3
  • 22
    • 0033525885 scopus 로고    scopus 로고
    • Structure of the complex between the antibiotic cerulenin and its target, β-ketoacyl-acyl carrier protein synthase
    • Moche M., Schneider G., Edwards P., Dehesh K., Lindqvist Y. Structure of the complex between the antibiotic cerulenin and its target, β-ketoacyl-acyl carrier protein synthase. J. Biol. Chem. 274:1999;6031-6034.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6031-6034
    • Moche, M.1    Schneider, G.2    Edwards, P.3    Dehesh, K.4    Lindqvist, Y.5
  • 23
    • 0024564710 scopus 로고
    • Acetoacetyl-acyl carrier protein synthase: A target for the antibiotic thiolactomycin
    • Jackowski S., Murphy C.M., Cronan J.E. Jr., Rock C.O. Acetoacetyl-acyl carrier protein synthase: a target for the antibiotic thiolactomycin. J. Biol. Chem. 264:1989;7624-7629.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7624-7629
    • Jackowski, S.1    Murphy, C.M.2    Cronan J.E., Jr.3    Rock, C.O.4
  • 24
    • 0026544037 scopus 로고
    • Overproduction of β-ketoacyl-acyl carrier protein synthase I imparts thiolactomycin resistance to Escherichia coli K-12
    • Tsay J.-T., Rock C.O., Jackowski S. Overproduction of β-ketoacyl-acyl carrier protein synthase I imparts thiolactomycin resistance to Escherichia coli K-12. J. Bacteriol. 174:1992;508-513.
    • (1992) J. Bacteriol. , vol.174 , pp. 508-513
    • Tsay, J.-T.1    Rock, C.O.2    Jackowski, S.3
  • 25
    • 0032473567 scopus 로고    scopus 로고
    • Crystal structure of β-ketoacyl-acyl carrier protein synthase II from E. coli reveals the molecular architecture of condensing enzymes
    • Huang W., Jia J., Edwards P., Dehesh K., Schneider G., Lindqvist Y. Crystal structure of β-ketoacyl-acyl carrier protein synthase II from E. coli reveals the molecular architecture of condensing enzymes. EMBO J. 17:1998;1183-1191.
    • (1998) EMBO J. , vol.17 , pp. 1183-1191
    • Huang, W.1    Jia, J.2    Edwards, P.3    Dehesh, K.4    Schneider, G.5    Lindqvist, Y.6
  • 26
    • 0032805888 scopus 로고    scopus 로고
    • Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis
    • Ferrer J.-L., Jez J.M., Bowman M.E., Dixon R.A., Noel J.P. Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Nat. Struct. Biol. 6:1999;775-784.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 775-784
    • Ferrer, J.-L.1    Jez, J.M.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 28
    • 0017881332 scopus 로고
    • The α-helix dipole and the properties of proteins
    • Hol W.G.J., van Duijnen P.T., Berendsen H.J.C. The α-helix dipole and the properties of proteins. Nature. 273:1978;443-446.
    • (1978) Nature , vol.273 , pp. 443-446
    • Hol, W.G.J.1    Van Duijnen, P.T.2    Berendsen, H.J.C.3
  • 29
    • 0028886558 scopus 로고
    • a values in proteins of the thioredoxin family
    • a values in proteins of the thioredoxin family. J. Mol. Biol. 253:1995;799-812.
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 30
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut J. Serine proteases: structure and mechanism of catalysis. Annu. Rev. Biochem. 46:1977;331-358.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J.1
  • 31
    • 0032584583 scopus 로고    scopus 로고
    • Functional characteristics of the oxyanion hole in human acetylcholinesterase
    • Ordentlich A., Shafferman A.et al. Functional characteristics of the oxyanion hole in human acetylcholinesterase. J. Biol. Chem. 273:1999;19509-19517.
    • (1999) J. Biol. Chem. , vol.273 , pp. 19509-19517
    • Ordentlich, A.1    Shafferman, A.2
  • 32
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L., Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20:1995;478-480.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 33
    • 0031592777 scopus 로고    scopus 로고
    • The 1.8 Å crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: Implications for substrate binding and reaction mechanism
    • Mathieu M., Wierenga R.K.et al. The 1.8 Å crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism. J. Mol. Biol. 273:1997;714-728.
    • (1997) J. Mol. Biol. , vol.273 , pp. 714-728
    • Mathieu, M.1    Wierenga, R.K.2
  • 34
    • 0001155699 scopus 로고
    • Metal-chelate affinity chromatography
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, & K. Strugh. New York: John Wiley & Sons, Inc
    • Petty K.J. Metal-chelate affinity chromatography. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Strugh K. Current Protocols in Molecular Biology. 1994;10.11.8-10.11.22 John Wiley & Sons, Inc, New York.
    • (1994) Current Protocols in Molecular Biology , pp. 10118-101122
    • Petty, K.J.1
  • 35
    • 0003785155 scopus 로고
    • New York: Cold Spring Harbor Laboratory, Cold Spring Harbor
    • Miller J.H. Experiments in Molecular Genetics. 1972;Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 36
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 39
    • 0030059608 scopus 로고    scopus 로고
    • Statistical expression value of the Debye-Waller factor and E(hkl) values for macromolecular crystals
    • Blessing R.H., Guo D.Y., Langs D.A. Statistical expression value of the Debye-Waller factor and E(hkl) values for macromolecular crystals. Acta Crystallogr. D. 52:1996;257-266.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 257-266
    • Blessing, R.H.1    Guo, D.Y.2    Langs, D.A.3
  • 41
    • 0001804798 scopus 로고
    • A minimal principle in the phase problem
    • D. Moras, A.D. Podjarny, & J.C. Thierry. Oxford, UK: IUCr and Oxford University Press
    • Hauptman H.A. A minimal principle in the phase problem. Moras D., Podjarny A.D., Thierry J.C. Crystallographic Computing 5: From Chemistry to Biology. 1991;324-332 IUCr and Oxford University Press, Oxford, UK.
    • (1991) Crystallographic Computing 5: From Chemistry to Biology , pp. 324-332
    • Hauptman, H.A.1
  • 42
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf, P.R. Evans, & A.G.W. Leslie. Warrington, UK: SERC Proceedings, Daresbury Laboratories
    • Otwinowski Z. Maximum likelihood refinement of heavy atom parameters. Wolf W., Evans P.R., Leslie A.G.W. Isomorphous Replacement and Anomalous Scattering. 1991;80-88 SERC Proceedings, Daresbury Laboratories, Warrington, UK.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-88
    • Otwinowski, Z.1
  • 44
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 45
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for binding 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
  • 46
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D. 53:1997;240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 48
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 49
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D. 55:1999;938-940.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.