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Volumn 1784, Issue 11, 2008, Pages 1847-1856

Versatile architecture of a bacterial aconitase B and its catalytic performance in the sequential reaction coupled with isocitrate dehydrogenase

Author keywords

Enzyme catalysis; Krebs cycle; Multienzyme complex; Protein protein interaction; Quaternary structure of protein; Small angle solution X ray scattering

Indexed keywords

ACONITATE HYDRATASE; ACONITATE HYDRATASE B; BACTERIAL ENZYME; HOMODIMER; HYBRID PROTEIN; ISOCITRATE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 54049149716     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.06.014     Document Type: Article
Times cited : (6)

References (32)
  • 1
    • 0037008011 scopus 로고    scopus 로고
    • Multiple conformational changes in enzyme catalysis
    • Hammes G.G. Multiple conformational changes in enzyme catalysis. Biochemistry 41 (2002) 8221-8228
    • (2002) Biochemistry , vol.41 , pp. 8221-8228
    • Hammes, G.G.1
  • 3
    • 54049148323 scopus 로고    scopus 로고
    • Controlling biomolecular diffusion: structural view of substrate channeling in fatty acid β-oxidation
    • Morikawa K., and Tate S. (Eds), Transworld Research Network, Kerala
    • Tsuchiya D., Ishikawa M., and Morikawa K. Controlling biomolecular diffusion: structural view of substrate channeling in fatty acid β-oxidation. In: Morikawa K., and Tate S. (Eds). Functional and Structural Biology on the Lipo-network (2006), Transworld Research Network, Kerala 117-133
    • (2006) Functional and Structural Biology on the Lipo-network , pp. 117-133
    • Tsuchiya, D.1    Ishikawa, M.2    Morikawa, K.3
  • 5
    • 24944549109 scopus 로고    scopus 로고
    • Interaction preferences across protein-protein interfaces of obligatory and non-obligatory components are different
    • De S., Krishnadev O., Srinivasan N., and Rekha N. Interaction preferences across protein-protein interfaces of obligatory and non-obligatory components are different. BMC Struct. Biol. 5 (2005) 15
    • (2005) BMC Struct. Biol. , vol.5 , pp. 15
    • De, S.1    Krishnadev, O.2    Srinivasan, N.3    Rekha, N.4
  • 6
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • Zimmerman S.B., and Trach S.O. Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J. Mol. Biol. 222 (1991) 599-620
    • (1991) J. Mol. Biol. , vol.222 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2
  • 7
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26 (2001) 597-604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 8
    • 0034161474 scopus 로고    scopus 로고
    • Macromolecular interactions: tracing the roots
    • Srere P.A. Macromolecular interactions: tracing the roots. Trends Biochem. Sci. 25 (2000) 150-153
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 150-153
    • Srere, P.A.1
  • 9
    • 0022515187 scopus 로고
    • Organization of citric acid cycle enzymes into a multienzyme cluster
    • Barnes S.J., and Weitzman P.D. Organization of citric acid cycle enzymes into a multienzyme cluster. FEBS Lett. 201 (1986) 267-270
    • (1986) FEBS Lett. , vol.201 , pp. 267-270
    • Barnes, S.J.1    Weitzman, P.D.2
  • 10
    • 0030069602 scopus 로고    scopus 로고
    • Identification of a multienzyme complex of the tricarboxylic acid cycle enzymes containing citrate synthase isoenzymes from Pseudomonas aeruginosa
    • Mitchell C.G. Identification of a multienzyme complex of the tricarboxylic acid cycle enzymes containing citrate synthase isoenzymes from Pseudomonas aeruginosa. Biochem. J. 313 Pt 3 (1996) 769-774
    • (1996) Biochem. J. , vol.313 , Issue.PART 3 , pp. 769-774
    • Mitchell, C.G.1
  • 11
    • 1642363933 scopus 로고    scopus 로고
    • Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli
    • Kumar J.K., Tabor S., and Richardson C.C. Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 3759-3764
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 3759-3764
    • Kumar, J.K.1    Tabor, S.2    Richardson, C.C.3
  • 13
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • Varghese S., Tang Y., and Imlay J.A. Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J. Bacteriol. 185 (2003) 221-230
    • (2003) J. Bacteriol. , vol.185 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 14
    • 19944400791 scopus 로고    scopus 로고
    • Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation
    • Tang Y., Guest J.R., Artymiuk P.J., and Green J. Switching aconitase B between catalytic and regulatory modes involves iron-dependent dimer formation. Mol. Microbiol. 56 (2005) 1149-1158
    • (2005) Mol. Microbiol. , vol.56 , pp. 1149-1158
    • Tang, Y.1    Guest, J.R.2    Artymiuk, P.J.3    Green, J.4
  • 16
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (A Complete Set of E. coli K-12 ORF Archive): unique resources for biological research
    • Kitagawa M., Ara T., Arifuzzaman M., Ioka-Nakamichi T., Inamoto E., Toyonaga H., and Mori H. Complete set of ORF clones of Escherichia coli ASKA library (A Complete Set of E. coli K-12 ORF Archive): unique resources for biological research. DNA Res. 12 (2005) 291-299
    • (2005) DNA Res. , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 17
    • 0033572854 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)
    • Jordan P.A., Tang Y., Bradbury A.J., Thomson A.J., and Guest J.R. Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB). Biochem. J. 344 Pt 3 (1999) 739-746
    • (1999) Biochem. J. , vol.344 , Issue.PART 3 , pp. 739-746
    • Jordan, P.A.1    Tang, Y.2    Bradbury, A.J.3    Thomson, A.J.4    Guest, J.R.5
  • 18
    • 0028952279 scopus 로고
    • Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP+-dependent isocitrate dehydrogenase from Escherichia coli
    • Lee M.E., Dyer D.H., Klein O.D., Bolduc J.M., Stoddard B.L., and Koshland Jr. D.E. Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP+-dependent isocitrate dehydrogenase from Escherichia coli. Biochemistry 34 (1995) 378-384
    • (1995) Biochemistry , vol.34 , pp. 378-384
    • Lee, M.E.1    Dyer, D.H.2    Klein, O.D.3    Bolduc, J.M.4    Stoddard, B.L.5    Koshland Jr., D.E.6
  • 21
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76 (1999) 2879-2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 22
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Cryst. 25 (1992) 495-503
    • (1992) J. Appl. Cryst. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 23
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89 (2005) 1237-1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 24
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D., Barberato C., and Koch M.H.J. CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Cryst. 28 (1995) 768-773
    • (1995) J. Appl. Cryst. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 25
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
    • CCP41
  • 26
    • 32044447203 scopus 로고    scopus 로고
    • Ligand-induced domain rearrangement of fatty acid β-oxidation multienzyme complex
    • Tsuchiya D., Shimizu N., Ishikawa M., Suzuki Y., and Morikawa K. Ligand-induced domain rearrangement of fatty acid β-oxidation multienzyme complex. Structure 14 (2006) 237-246
    • (2006) Structure , vol.14 , pp. 237-246
    • Tsuchiya, D.1    Shimizu, N.2    Ishikawa, M.3    Suzuki, Y.4    Morikawa, K.5
  • 27
    • 34248363563 scopus 로고    scopus 로고
    • Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography
    • Tsutakawa S.E., Hura G.L., Frankel K.A., Cooper P.K., and Tainer J.A. Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography. J. Struct. Biol. 158 (2007) 214-223
    • (2007) J. Struct. Biol. , vol.158 , pp. 214-223
    • Tsutakawa, S.E.1    Hura, G.L.2    Frankel, K.A.3    Cooper, P.K.4    Tainer, J.A.5
  • 28
    • 0031033691 scopus 로고    scopus 로고
    • The aconitase family: three structural variations on a common theme
    • Gruer M.J., Artymiuk P.J., and Guest J.R. The aconitase family: three structural variations on a common theme. Trends Biochem. Sci. 22 (1997) 3-6
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 3-6
    • Gruer, M.J.1    Artymiuk, P.J.2    Guest, J.R.3
  • 31
    • 0036225829 scopus 로고    scopus 로고
    • Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression
    • Tang Y., Quail M.A., Artymiuk P.J., Guest J.R., and Green J. Escherichia coli aconitases and oxidative stress: post-transcriptional regulation of sodA expression. Microbiology 148 (2002) 1027-1037
    • (2002) Microbiology , vol.148 , pp. 1027-1037
    • Tang, Y.1    Quail, M.A.2    Artymiuk, P.J.3    Guest, J.R.4    Green, J.5
  • 32
    • 0026612756 scopus 로고
    • Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin
    • Bashford D., and Gerwert K. Electrostatic calculations of the pKa values of ionizable groups in bacteriorhodopsin. J. Mol. Biol. 224 (1992) 473-486
    • (1992) J. Mol. Biol. , vol.224 , pp. 473-486
    • Bashford, D.1    Gerwert, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.