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Volumn 14, Issue 2, 2006, Pages 237-246

Ligand-induced domain rearrangement of fatty acid β-oxidation multienzyme complex

Author keywords

[No Author keywords available]

Indexed keywords

COENZYME A; MULTIENZYME COMPLEX; NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 32044447203     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.10.011     Document Type: Article
Times cited : (11)

References (33)
  • 2
    • 0034282901 scopus 로고    scopus 로고
    • Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase
    • J.J. Barycki, L.K. O'Brien, A.W. Strauss, and L.J. Banaszak Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase J. Biol. Chem. 275 2000 27186 27196
    • (2000) J. Biol. Chem. , vol.275 , pp. 27186-27196
    • Barycki, J.J.1    O'Brien, L.K.2    Strauss, A.W.3    Banaszak, L.J.4
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallgr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallgr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 5
    • 2342525085 scopus 로고    scopus 로고
    • Heterogeneity and inaccuracy in protein structures solved by X-ray crystallography
    • M. DePristro, P.I.W. de Bakker, and T.L. Blundell Heterogeneity and inaccuracy in protein structures solved by X-ray crystallography Structure 12 2004 831 838
    • (2004) Structure , vol.12 , pp. 831-838
    • Depristro, M.1    De Bakker, P.I.W.2    Blundell, T.L.3
  • 9
    • 0031439913 scopus 로고    scopus 로고
    • Reconstitution, morphology and crystallization of a fatty acid β-oxidation multienzyme complex from Pseudomonas fragi
    • M. Ishikawa, Y. Mikami, J. Usukura, H. Iwasaki, H. Shinagawa, and K. Morikawa Reconstitution, morphology and crystallization of a fatty acid β-oxidation multienzyme complex from Pseudomonas fragi Biochem. J. 328 1997 815 820
    • (1997) Biochem. J. , vol.328 , pp. 815-820
    • Ishikawa, M.1    Mikami, Y.2    Usukura, J.3    Iwasaki, H.4    Shinagawa, H.5    Morikawa, K.6
  • 10
    • 3543016798 scopus 로고    scopus 로고
    • Structural basis for channelling mechanism of a fatty acid β-oxidation multienzyme complex
    • M. Ishikawa, D. Tsuchiya, T. Oyama, Y. Tsunaka, and K. Morikawa Structural basis for channelling mechanism of a fatty acid β-oxidation multienzyme complex EMBO J. 23 2004 2745 2754
    • (2004) EMBO J. , vol.23 , pp. 2745-2754
    • Ishikawa, M.1    Tsuchiya, D.2    Oyama, T.3    Tsunaka, Y.4    Morikawa, K.5
  • 11
    • 0036913740 scopus 로고    scopus 로고
    • Burning fat: The structural basis of fatty acid β-oxidation
    • J.J. Kim, and K.P. Battaile Burning fat: the structural basis of fatty acid β-oxidation Curr. Opin. Struct. Biol. 12 2002 721 728
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 721-728
    • Kim, J.J.1    Battaile, K.P.2
  • 12
    • 0034849689 scopus 로고    scopus 로고
    • MASSHA: A graphics system for rigid-body modelling of macromolecular complexes against solution scattering data
    • P.V. Konarev, M.V. Petoukhov, and D.I. Svergun MASSHA: a graphics system for rigid-body modelling of macromolecular complexes against solution scattering data J. Appl. Crystallogr. 34 2001 527 532
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 527-532
    • Konarev, P.V.1    Petoukhov, M.V.2    Svergun, D.I.3
  • 13
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.E. Kraulis 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.E.1
  • 15
    • 14144254724 scopus 로고    scopus 로고
    • High resolution crystal structures of human cytosolic thiolase (CT): A comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I
    • P. Kursula, H. Sikkila, T. Fukao, N. Kondo, and R.K. Wierenga High resolution crystal structures of human cytosolic thiolase (CT): a comparison of the active sites of human CT, bacterial thiolase, and bacterial KAS I J. Mol. Biol. 347 2005 189 201
    • (2005) J. Mol. Biol. , vol.347 , pp. 189-201
    • Kursula, P.1    Sikkila, H.2    Fukao, T.3    Kondo, N.4    Wierenga, R.K.5
  • 16
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • S.J. Lin, and L. Guarente Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease Curr. Opin. Cell Biol. 15 2003 241 246
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 18
    • 0028144138 scopus 로고
    • Aspartate transcarbamoylase from Escherichia coli: Activity and regulation
    • W.N. Lipscomb Aspartate transcarbamoylase from Escherichia coli: activity and regulation Adv. Enzymol. Relat. Areas Mol. Biol. 68 1994 67 151
    • (1994) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.68 , pp. 67-151
    • Lipscomb, W.N.1
  • 19
    • 0035036495 scopus 로고    scopus 로고
    • Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase
    • C.P. Macol, H. Tsuruta, B. Stec, and E.R. Kantrowitz Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase Nat. Struct. Biol. 8 2001 423 426
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 423-426
    • MacOl, C.P.1    Tsuruta, H.2    Stec, B.3    Kantrowitz, E.R.4
  • 20
    • 0028174351 scopus 로고
    • The 2.8 Å crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: A five-layered αβαβα structure constructed from two core domains of identical topology
    • M. Mathieu, J.P. Zeelen, R.A. Pauptit, R. Erdmann, W.H. Kunau, and R.K. Wierenga The 2.8 Å crystal structure of peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: a five-layered αβαβ α structure constructed from two core domains of identical topology Structure 2 1994 797 808
    • (1994) Structure , vol.2 , pp. 797-808
    • Mathieu, M.1    Zeelen, J.P.2    Pauptit, R.A.3    Erdmann, R.4    Kunau, W.H.5    Wierenga, R.K.6
  • 22
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D version 2.0: A program for photorealistic molecular graphics
    • E.A. Merrit, and D.J. Bacon Raster3D version 2.0: a program for photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 23
    • 0033569705 scopus 로고    scopus 로고
    • A biosynthetic thiolase in complex with a reaction intermediate: The crystal structure provides new insights into the catalytic mechanism
    • Y. Modis, and R.K. Wierenga A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism Struct. Fold. Des. 7 1998 1279 1290
    • (1998) Struct. Fold. Des. , vol.7 , pp. 1279-1290
    • Modis, Y.1    Wierenga, R.K.2
  • 24
    • 13844253947 scopus 로고    scopus 로고
    • SAXS and the working protein
    • B. Nagar, and J. Kuriyan SAXS and the working protein Structure 13 2005 169 170
    • (2005) Structure , vol.13 , pp. 169-170
    • Nagar, B.1    Kuriyan, J.2
  • 25
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navaza AMoRe: an automated package for molecular replacement Acta Crystallogr. A50 1994 157 163
    • (1994) Acta Crystallogr. , vol.50 , pp. 157-163
    • Navaza, J.1
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter Jr. R.M. Sweet Academic Press New York
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter Jr. R.M. Sweet Methods in Enzymology, Volume 276 1997 Academic Press New York 307 326
    • (1997) Methods in Enzymology, Volume 276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0037701771 scopus 로고    scopus 로고
    • New methods for domain structure determination of proteins from solution scattering data
    • M.V. Petoukhov, and D.I. Svergun New methods for domain structure determination of proteins from solution scattering data J. Appl. Crystallogr. 36 2003 540 544
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 540-544
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 29
    • 0029185933 scopus 로고
    • CRYSOL: A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • D. Svergun, C. Barberato, and M.H. Koch CRYSOL: a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 30
    • 18144362422 scopus 로고    scopus 로고
    • Substrate-induced interconversion of protein quaternary structure isoforms
    • L. Tang, L. Stith, and E.K. Jaffe Substrate-induced interconversion of protein quaternary structure isoforms J. Biol. Chem. 280 2005 15786 15793
    • (2005) J. Biol. Chem. , vol.280 , pp. 15786-15793
    • Tang, L.1    Stith, L.2    Jaffe, E.K.3
  • 32
    • 32044450629 scopus 로고    scopus 로고
    • Solution X-ray scattering analysis of fatty acid β-oxidation multienzyme complex
    • Tsuchiya, D., Suzuki, Y., Shimizu, N., Ishikawa, M., and Morikawa, K. (2004). Solution X-ray scattering analysis of fatty acid β-oxidation multienzyme complex. SPring-8 User Experiment Report, http://www.spring8.or.jp/ e/publication/UER03B/178.pdf 12, 178.
    • (2004) SPring-8 User Experiment Report , vol.12 , pp. 178
    • Tsuchiya, D.1    Suzuki, Y.2    Shimizu, N.3    Ishikawa, M.4    Morikawa, K.5
  • 33
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • S.B. Zimmerman, and S.O. Trach 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.