메뉴 건너뛰기




Volumn 185, Issue 14, 2003, Pages 4136-4143

The 1.3-Angstrom-resolution crystal structure of β-ketoacyl-acyl carrier protein synthase II from Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

3 OXOACYL ACYL CARRIER PROTEIN SYNTHASE; CARRIER PROTEIN;

EID: 0038154085     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.14.4136-4143.2003     Document Type: Article
Times cited : (49)

References (50)
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computation Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50:760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 6
    • 0015819138 scopus 로고
    • Inhibition of fatty acid biosynthesis by the antibiotic cerulenin. Specific inactivation of β-ketoacyl-acyl carrier protein synthetase
    • D'Agnolo, G., I. S. Rosenfeld, J. Awaya, S. Omura, and P. R. Vagelos. 1973. Inhibition of fatty acid biosynthesis by the antibiotic cerulenin. Specific inactivation of β-ketoacyl-acyl carrier protein synthetase. Biochim. Biophys. Acta 326:155-166.
    • (1973) Biochim. Biophys. Acta , vol.326 , pp. 155-166
    • D'Agnolo, G.1    Rosenfeld, I.S.2    Awaya, J.3    Omura, S.4    Vagelos, P.R.5
  • 7
    • 0016734774 scopus 로고
    • Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli
    • D'Agnolo, G., I. S. Rosenfeld, and P. R. Vagelos. 1975. Multiple forms of β-ketoacyl-acyl carrier protein synthetase in Escherichia coli. J. Biol. Chem. 250:5289-5294.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5289-5294
    • D'Agnolo, G.1    Rosenfeld, I.S.2    Vagelos, P.R.3
  • 8
    • 0034651317 scopus 로고    scopus 로고
    • The 1.8 Å crystal structure and active site architecture of β-ketoacyl-[acyl carrier protein] synthase III (FabH) from Escherichia coli
    • Davies, C., R. J. Heath, S. W. White, and C. O. Rock. 2000. The 1.8 Å crystal structure and active site architecture of β-ketoacyl-[acyl carrier protein] synthase III (FabH) from Escherichia coli. Structure 8:185-195.
    • (2000) Structure , vol.8 , pp. 185-195
    • Davies, C.1    Heath, R.J.2    White, S.W.3    Rock, C.O.4
  • 9
    • 0036178630 scopus 로고    scopus 로고
    • The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1
    • Davies, D. R., H. Interthal, J. J. Cbampoux, and W. G. Hol. 2002. The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1. Structure 10:237-248.
    • (2002) Structure , vol.10 , pp. 237-248
    • Davies, D.R.1    Interthal, H.2    Cbampoux, J.J.3    Hol, W.G.4
  • 10
    • 0344250735 scopus 로고
    • Thermal regulation of membrane lipid fluidity in bacteria
    • de Mendoza, D., and J. E. Cronan, Jr. 1983. Thermal regulation of membrane lipid fluidity in bacteria. Trends Biochem. Sci. 8:49-52.
    • (1983) Trends Biochem. Sci. , vol.8 , pp. 49-52
    • De Mendoza, D.1    Cronan J.E., Jr.2
  • 12
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R. M. 1999. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D 55:938-940.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 13
    • 0032805888 scopus 로고    scopus 로고
    • Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis
    • Ferrer, J.-L., J. M. Jez, M. E. Bowman, R. A. Dixon, and J. P. Noel. 1999. Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Nat. Struct. Biol. 6:775-784.
    • (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
  • 14
    • 0018969670 scopus 로고
    • β-ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis
    • Garwin, J. L., A. L. Klages, and J. E. Cronan, Jr. 1980. β-Ketoacyl-acyl carrier protein synthase II of Escherichia coli. Evidence for function in the thermal regulation of fatty acid synthesis. J. Biol. Chem. 255:3263-3265.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3263-3265
    • Garwin, J.L.1    Klages, A.L.2    Cronan J.E., Jr.3
  • 15
    • 0036775842 scopus 로고    scopus 로고
    • The Claisen condensation in biology
    • Heath, R. J., and C. O. Rock. 2002. The Claisen condensation in biology. Nat. Prod. Rep. 19:581-596.
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 581-596
    • Heath, R.J.1    Rock, C.O.2
  • 16
    • 0034804919 scopus 로고    scopus 로고
    • Lipid biosynthesis as a target for antibacterial agents
    • Heath, R. J., S. W. White, and C. O. Rock. 2001. Lipid biosynthesis as a target for antibacterial agents. Prog. Lipid Res. 40:467-497.
    • (2001) Prog. Lipid Res. , vol.40 , pp. 467-497
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 17
    • 0032515066 scopus 로고    scopus 로고
    • Broad spectrum antimicrobial biocides target the FabI component of fatty acid synthesis
    • Heath, R. J., Y.-T. Yu, M. A. Shapiro, E. Olson, and C. O. Rock. 1998. Broad spectrum antimicrobial biocides target the FabI component of fatty acid synthesis. J. Biol. Chem. 273:30316-30321.
    • (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
  • 18
    • 0025606149 scopus 로고
    • Molecular genetics of polyketides and its comparison to fatty acid biosynthesis
    • Hopwood, D. A., and D. H. Sherman. 1990. Molecular genetics of polyketides and its comparison to fatty acid biosynthesis. Annu. Rev. Genet. 24:37-66.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 37-66
    • Hopwood, D.A.1    Sherman, D.H.2
  • 19
    • 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., J. Jia, P. Edwards, K. Dehesh, G. Schneider, and Y. Lindqvist. 1998. Crystal structure of β-ketoacyl-acyl carrier protein synthase II from E. coli reveals the molecular architecture of condensing enzymes. EMBO J. 17:1183-1191.
    • (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
  • 20
    • 0023644886 scopus 로고
    • Acetoacetyl-acyl carrier protein synthase, a potential regulator of fatty acid biosynthesis in bacteria
    • Jackowski, S., and C. O. Rock. 1987. Acetoacetyl-acyl carrier protein synthase, a potential regulator of fatty acid biosynthesis in bacteria. J. Biol. Chem. 262:7927-7931.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7927-7931
    • Jackowski, S.1    Rock, C.O.2
  • 22
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47:110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 25
    • 0038242930 scopus 로고    scopus 로고
    • Cholesterol biosynthesis
    • D. E. Vance and J. E. Vance (ed.). Elsevier, New York, N.Y.
    • Liscum, L. 2002. Cholesterol biosynthesis, p. 409-431. In D. E. Vance and J. E. Vance (ed.), Biochemistry of lipids, lipoproteins and membranes, 4th ed. Elsevier, New York, N.Y.
    • (2002) Biochemistry of Lipids, Lipoproteins and Membranes, 4th Ed. , pp. 409-431
    • Liscum, L.1
  • 26
    • 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., Y. Modis, J. P. Zeelen, C. K. Engel, R. A. Abagyan, A. Ahlberg, B. Rasmussen, V. S. Lamzin, W. H. Kunau, and R. K. Wierenga. 1997. 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. 273:714-728.
    • (1997) J. Mol. Biol. , vol.273 , pp. 714-728
    • Mathieu, M.1    Modis, Y.2    Zeelen, J.P.3    Engel, C.K.4    Abagyan, R.A.5    Ahlberg, A.6    Rasmussen, B.7    Lamzin, V.S.8    Kunau, W.H.9    Wierenga, R.K.10
  • 27
    • 0035928728 scopus 로고    scopus 로고
    • β-ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: Aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket
    • McGuire, K. A., M. Siggaard-Andersen, M. G. Bangera, J. G. Olsen, and P. Wettstein-Knowles. 2001. β-Ketoacyl-[acyl carrier protein] synthase I of Escherichia coli: aspects of the condensation mechanism revealed by analyses of mutations in the active site pocket. Biochemistry 40:9836-9845.
    • (2001) Biochemistry , vol.40 , pp. 9836-9845
    • McGuire, K.A.1    Siggaard-Andersen, M.2    Bangera, M.G.3    Olsen, J.G.4    Wettstein-Knowles, P.5
  • 29
    • 0030815133 scopus 로고    scopus 로고
    • Rasater 3D: Photorealistic molecular graphics
    • Merrit, E. A., and D. J. Bacon. 1997. Rasater 3D: photorealistic molecular graphics. Methods Enzymol. 277:505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 31
    • 0035910286 scopus 로고    scopus 로고
    • The crystal structure of β-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54 A resolution and its relationship to other condensing enzymes
    • Moche, M., K. Dehesh, P. Edwards, and Y. Lindqvist. 2001. The crystal structure of β-ketoacyl-acyl carrier protein synthase II from Synechocystis sp. at 1.54 A resolution and its relationship to other condensing enzymes. J. Mol. Biol. 305:491-503.
    • (2001) J. Mol. Biol. , vol.305 , pp. 491-503
    • Moche, M.1    Dehesh, K.2    Edwards, P.3    Lindqvist, Y.4
  • 32
    • 0033525885 scopus 로고    scopus 로고
    • Structure of the complex between the antibiotic cerulenin and its target, β-ketoacyl-acyl carrier protein synthase
    • Moche, M., G. Schneider, P. Edwards, K. Dehesh, and Y. Lindqvist. 1999. Structure of the complex between the antibiotic cerulenin and its target, β-ketoacyl-acyl carrier protein synthase. J. Biol. Chem. 274:6031-6034.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6031-6034
    • Moche, M.1    Schneider, G.2    Edwards, P.3    Dehesh, K.4    Lindqvist, Y.5
  • 33
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., A. A. Vagin, and E. J. Dodson. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53:240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 34
    • 84920325457 scopus 로고
    • AMoRe - An automated package for molecular replacement
    • Navaza, J. 1994. AMoRe - an automated package for molecular replacement. Acta Crystallogr. A 50:869-873.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 869-873
    • Navaza, J.1
  • 35
    • 0035085234 scopus 로고    scopus 로고
    • Structures of β-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery
    • Olsen, J. G., A. Kadziola, P. Wettstein-Knowles, M. Siggaard-Andersen, and S. Larsen. 2001. Structures of β-ketoacyl-acyl carrier protein synthase I complexed with fatty acids elucidate its catalytic machinery. Structure 9:233-243.
    • (2001) Structure , vol.9 , pp. 233-243
    • Olsen, J.G.1    Kadziola, A.2    Wettstein-Knowles, P.3    Siggaard-Andersen, M.4    Larsen, S.5
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0035794127 scopus 로고    scopus 로고
    • Inhibition of β-ketoacyl-[acyl carrier protein] synthases by thiolactomycin and cerulenin: Structure and mechanism
    • Price, A. C., K. H. Choi, R. J. Heath, Z. Li, C. O. Rock, and S. W. White. 2001. Inhibition of β-ketoacyl-[acyl carrier protein] synthases by thiolactomycin and cerulenin: structure and mechanism. J. Biol. Chem. 276:6551-6559.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6551-6559
    • Price, A.C.1    Choi, K.H.2    Heath, R.J.3    Li, Z.4    Rock, C.O.5    White, S.W.6
  • 42
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock, C. O., and J. E. Cronan, Jr. 1996. Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta 1302:1-16.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan J.E., Jr.2
  • 43
    • 0015919605 scopus 로고
    • Synthesis of unsaturated fatty acids and the lesion in fabB mutants
    • Rosenfeld, I. S., G. D'Agnolo, and P. R. Vagelos. 1973. Synthesis of unsaturated fatty acids and the lesion in fabB mutants. J. Biol. Chem. 248:2452-2460.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2452-2460
    • Rosenfeld, I.S.1    D'Agnolo, G.2    Vagelos, P.R.3
  • 45
    • 0035827542 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III
    • Scarsdale, J. N., G. Kazanina, X. He, K. A. Reynolds, and H. T. Wright. 2001. Crystal structure of the Mycobacterium tuberculosis β-ketoacyl-acyl carrier protein synthase III. J. Biol. Chem. 276:20516-20522.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20516-20522
    • Scarsdale, J.N.1    Kazanina, G.2    He, X.3    Reynolds, K.A.4    Wright, H.T.5
  • 46
    • 0037905519 scopus 로고    scopus 로고
    • Oxidation of fatty acid in eukaryotes
    • D. E. Vance and J. E. Vance (ed.). Elsevier, New York, N.Y.
    • Schulz, H. 2002. Oxidation of fatty acid in eukaryotes, p. 127-180. In D. E. Vance and J. E. Vance (ed.), Biochemistry of lipids, lipoproteins and membranes, 4th ed. Elsevier, New York, N.Y.
    • (2002) Biochemistry of Lipids, Lipoproteins and Membranes, 4th Ed. , pp. 127-180
    • Schulz, H.1
  • 47
    • 0028557012 scopus 로고
    • The animal fatty acid synthase: One gene, one polypeptide, seven enzymes
    • Smith, S. 1994. The animal fatty acid synthase: one gene, one polypeptide, seven enzymes. FASEB J. 8:1248-1259.
    • (1994) FASEB J. , vol.8 , pp. 1248-1259
    • Smith, S.1
  • 49
    • 0026544037 scopus 로고
    • Overproduction of β-ketoacyl-acyl carrier protein synthase I imparts thiolactomycin resistance to Escherichia coli K-12
    • Tsay, J.-T., C. O. Rock, and S. Jackowski. 1992. Overproduction of β-ketoacyl-acyl carrier protein synthase I imparts thiolactomycin resistance to Escherichia coli K-12. J. Bacteriol. 174:508-513.
    • (1992) J. Bacteriol. , vol.174 , pp. 508-513
    • Tsay, J.-T.1    Rock, C.O.2    Jackowski, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.