메뉴 건너뛰기




Volumn 6, Issue 8, 1998, Pages 957-970

The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate sidechains for catalysis

Author keywords

Import; Isomerase; Mitochondria; Peroxisome; oxidation

Indexed keywords

ANIMALIA;

EID: 0032528950     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00098-7     Document Type: Article
Times cited : (83)

References (54)
  • 1
    • 0342528190 scopus 로고
    • Fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a prypolipidemic drug
    • Lazarow, P.B. & de Duve, C. (1976). Fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a prypolipidemic drug. Proc. Natl. Acad. Sci. USA 73, 2043-2046.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2043-2046
    • Lazarow, P.B.1    De Duve, C.2
  • 2
    • 0004155427 scopus 로고
    • W. H. Freeman and Company, New York, USA
    • Stryer, L. (1988). In Biochemistry. W. H. Freeman and Company, New York, USA. pp 469-493.
    • (1988) Biochemistry , pp. 469-493
    • Stryer, L.1
  • 3
    • 0014690479 scopus 로고
    • Studies on the α-oxidation of phytanic acid by rat liver mitochondria
    • Tsai, S.-C., Avignan, J. & Steinberg, D. (1969). Studies on the α-oxidation of phytanic acid by rat liver mitochondria. J. Biol. Chem. 244, 2682-2692.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2682-2692
    • Tsai, S.-C.1    Avignan, J.2    Steinberg, D.3
  • 4
    • 0026329270 scopus 로고
    • Identification and purification of a peroxisomal branched chain fatty acyl-CoA oxidase
    • van Veldhoven, P.P. et al., & Mannaerts, G.P. (1991). Identification and purification of a peroxisomal branched chain fatty acyl-CoA oxidase. J. Biol. Chem. 266, 24676-24683.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24676-24683
    • Van Veldhoven, P.P.1    Mannaerts, G.P.2
  • 5
    • 0026200272 scopus 로고
    • Mitochondrial 3-2trans-enoyl-CoA isomerase. Purification, cloning, expression, and mitochondrial import of the key enzyme of unsaturated fatty acid β-oxidation
    • Müller-Newen, G. & Stoffel, W. (1991). Mitochondrial 3-2trans-enoyl-CoA isomerase. Purification, cloning, expression, and mitochondrial import of the key enzyme of unsaturated fatty acid β-oxidation. Biol. Chem. Hoppe Seyler 372, 613-624.
    • (1991) Biol. Chem. Hoppe Seyler , vol.372 , pp. 613-624
    • Müller-Newen, G.1    Stoffel, W.2
  • 6
    • 0025954516 scopus 로고
    • NADPH-dependent reductive metabolism of cis-5 unsaturated fatty acids
    • Tserng, K.Y. & Jin, S.J. (1991 ). NADPH-dependent reductive metabolism of cis-5 unsaturated fatty acids. J. Biol. Chem. 266, 11614-11620.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11614-11620
    • Tserng, K.Y.1    Jin, S.J.2
  • 7
    • 0028176487 scopus 로고
    • Purification and properties of an a-methylacyl-CoA racemase from rat liver
    • Schmitz, W., Fingerhut, R. & Conzelmann, E. (1994). Purification and properties of an a-methylacyl-CoA racemase from rat liver. Eur. J. Biochem. 222, 313-323.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 313-323
    • Schmitz, W.1    Fingerhut, R.2    Conzelmann, E.3
  • 10
    • 0028970515 scopus 로고
    • 2,4-dienoyl-CoA isomerase and thus possess all enzymes required for the β-oxidation of unsaturated fatty acids by a novel reductase-dependent pathway
    • 2,4-dienoyl-CoA isomerase and thus possess all enzymes required for the β-oxidation of unsaturated fatty acids by a novel reductase-dependent pathway. Biochem. Biophys. Res. Commun. 215, 15-22.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 15-22
    • He, X.-Y.1    Shoukry, K.2    Chu, C.3    Yang, J.4    Sprecher, H.5    Schulz, H.6
  • 11
    • 0019783299 scopus 로고
    • Degradation of unsaturated fatty acids in peroxisomes
    • Dommes, V., Baumgart, C. and Kunau, W.-H. (1981). Degradation of unsaturated fatty acids in peroxisomes. J. Biol. Chem. 256, 8259-8262.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8259-8262
    • Dommes, V.1    Baumgart, C.2    Kunau, W.-H.3
  • 14
    • 0029048150 scopus 로고
    • Isolation and characterization of rat and human cDNAs encoding a novel putative peroxisomal enoyl-CoA hydratase
    • FitzPatrick, D.R., Germain-Lee, E. & Valle, D. (1995). Isolation and characterization of rat and human cDNAs encoding a novel putative peroxisomal enoyl-CoA hydratase. Genomics 27, 457-466.
    • (1995) Genomics , vol.27 , pp. 457-466
    • FitzPatrick, D.R.1    Germain-Lee, E.2    Valle, D.3
  • 15
    • 0031594712 scopus 로고    scopus 로고
    • 2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization
    • 2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization. J. Biol. Chem. 273, 349-355.
    • (1998) J. Biol. Chem. , vol.273 , pp. 349-355
    • Filppula, S.A.1    Hiltunen, J.K.2
  • 16
  • 17
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: A spiral fold defines the CoA-binding pocket
    • Engel, C.K., Mathieu, M., Zeelen, J.P., Hiltunen, J.K. & Wierenga, R.K. (1996). Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: a spiral fold defines the CoA-binding pocket. EMBO J. 15, 5135-5145.
    • (1996) EMBO J. , vol.15 , pp. 5135-5145
    • Engel, C.K.1    Mathieu, M.2    Zeelen, J.P.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 18
    • 0030037645 scopus 로고    scopus 로고
    • Structure of 4-chlorobenzoyl-coenzyme A dehalogenase determined to 1.8 Å resolution: An enzyme catalyst via adaptive mutation
    • Benning, M.M. et al., & Holden, H.M. (1996). Structure of 4-chlorobenzoyl-coenzyme A dehalogenase determined to 1.8 Å resolution: an enzyme catalyst via adaptive mutation. Biochemistry 35, 8103-8109.
    • (1996) Biochemistry , vol.35 , pp. 8103-8109
    • Benning, M.M.1    Holden, H.M.2
  • 19
    • 0014691284 scopus 로고
    • The subunit structure of crotonase
    • Hass, G.M. & Hill, R.L. (1969). The subunit structure of crotonase. J. Biol. Chem. 244, 6080-6086.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6080-6086
    • Hass, G.M.1    Hill, R.L.2
  • 20
    • 0032488815 scopus 로고    scopus 로고
    • The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule
    • Engel, C.K., Kiema, T.R., Hiltunen, J.K. & Wierenga, R.K. (1998). The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule. J. Mol. Biol. 275, 847-859.
    • (1998) J. Mol. Biol. , vol.275 , pp. 847-859
    • Engel, C.K.1    Kiema, T.R.2    Hiltunen, J.K.3    Wierenga, R.K.4
  • 21
    • 0027955787 scopus 로고
    • Biased Probability Monte Carlo conformational searches and electrostatics calculations for peptides and proteins
    • Abagyan, R. & Totrov, M. (1994). Biased Probability Monte Carlo conformational searches and electrostatics calculations for peptides and proteins. J. Mol. Biol. 235, 983-1002.
    • (1994) J. Mol. Biol. , vol.235 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 22
    • 0028972337 scopus 로고
    • Strange bedfellows: Interactions between acidic sidechains in proteins
    • Flocco, M.M. & Mowbray, S.L. (1995). Strange bedfellows: Interactions between acidic sidechains in proteins. J. Mol. Biol. 254, 96-105.
    • (1995) J. Mol. Biol. , vol.254 , pp. 96-105
    • Flocco, M.M.1    Mowbray, S.L.2
  • 23
    • 0030766386 scopus 로고    scopus 로고
    • Glutamate-119 of the large alpha-subunit is the catalytic base in the hydration of 2-trans-enoyl-coenzyme A catalyzed by the mutienzyme complex of fatty acid oxidation from Escherichia coli
    • He, X.Y. & Yang, S.Y. (1 997). Glutamate-119 of the large alpha-subunit is the catalytic base in the hydration of 2-trans-enoyl-coenzyme A catalyzed by the mutienzyme complex of fatty acid oxidation from Escherichia coli. Biochemistry 36, 11044-11049.
    • (1997) Biochemistry , vol.36 , pp. 11044-11049
    • He, X.Y.1    Yang, S.Y.2
  • 24
    • 0027467033 scopus 로고
    • The α-aneurism: A structural motif revealed in an insertion mutant of staphylococcal nuclease
    • Keefe, L.J., Sondek, J., Shortle, D. & Lattman, E.E. (1993). The α-aneurism: a structural motif revealed in an insertion mutant of staphylococcal nuclease. Proc. Natl Acad. Sci. USA 90, 3275-3279.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3275-3279
    • Keefe, L.J.1    Sondek, J.2    Shortle, D.3    Lattman, E.E.4
  • 25
    • 0029976299 scopus 로고    scopus 로고
    • Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria
    • Ashmarina, L.I., Robert, M.-F., Elsliger, M.-A. & Mitchell, G.A. (1996). Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria. Biochem. J. 315, 71-75.
    • (1996) Biochem. J. , vol.315 , pp. 71-75
    • Ashmarina, L.I.1    Robert, M.-F.2    Elsliger, M.-A.3    Mitchell, G.A.4
  • 26
    • 10144261887 scopus 로고    scopus 로고
    • A unified nomenclature for peroxisome biogenesis factors
    • Distel, B. et al., & Veenhuis, M. (1996). A unified nomenclature for peroxisome biogenesis factors. J. Cell Biol. 135, 1-3.
    • (1996) J. Cell Biol. , vol.135 , pp. 1-3
    • Distel, B.1    Veenhuis, M.2
  • 27
    • 0030781431 scopus 로고    scopus 로고
    • Active unfolding of precursor proteins during mitochondrial protein import
    • Matouschek, A., Azem, A., Ratliff, K., Glick, B.S., Schmid, K. & Schatz, G. (1997). Active unfolding of precursor proteins during mitochondrial protein import. EMBO J. 16, 6727-6736.
    • (1997) EMBO J. , vol.16 , pp. 6727-6736
    • Matouschek, A.1    Azem, A.2    Ratliff, K.3    Glick, B.S.4    Schmid, K.5    Schatz, G.6
  • 28
    • 0030969942 scopus 로고    scopus 로고
    • Protein Import into Mitochondria
    • Neupert, W. (1997). Protein Import into Mitochondria. Annu. Rev. Biochem. 66, 863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 29
    • 0030613780 scopus 로고    scopus 로고
    • 1-ATPase β-subunit precursor functions as an intramolecular chaperone to facilitate mitochondrial protein import
    • 1-ATPase β-subunit precursor functions as an intramolecular chaperone to facilitate mitochondrial protein import. Mol. Cell. Biol. 17, 7169-7177.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7169-7177
    • Hàjek, P.1    Koh, J.Y.2    Jones, L.3    Bedwell, D.M.4
  • 31
    • 0001305507 scopus 로고    scopus 로고
    • 5-3-ketosteroid isomerase with and without a reaction intermediate analogue
    • 5-3-ketosteroid isomerase with and without a reaction intermediate analogue. Biochemistry 36, 14030-14036.
    • (1997) Biochemistry , vol.36 , pp. 14030-14036
    • Kim, S.W.1    Oh, B.-H.2
  • 32
    • 0027382865 scopus 로고
    • Site-directed mutagenesis of putative active-site amino acid residues of 3,2-trans-enoyl-CoA isomerase, conserved within the low-homology isomerase/hydratase enzyme family
    • Müller-Newen, G. & Stoffel, W. (1993). Site-directed mutagenesis of putative active-site amino acid residues of 3,2-trans-enoyl-CoA isomerase, conserved within the low-homology isomerase/hydratase enzyme family. Biochemistry 32, 11405-11412.
    • (1993) Biochemistry , vol.32 , pp. 11405-11412
    • Müller-Newen, G.1    Stoffel, W.2
  • 33
    • 0026027728 scopus 로고
    • Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution
    • Klein, C. & Schulz, G.E. (1991). Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution. J. Mol. Biol. 217, 737-750.
    • (1991) J. Mol. Biol. , vol.217 , pp. 737-750
    • Klein, C.1    Schulz, G.E.2
  • 35
    • 0031017915 scopus 로고    scopus 로고
    • Investigation of substrate activation by 4-chlorobenzoyl-coenzyme A dehalogenase
    • Taylor, K.L., Xiang, H., Liu, R.-Q., Yang, G. & Dunaway-Mariano, D. (1997). Investigation of substrate activation by 4-chlorobenzoyl-coenzyme A dehalogenase. Biochemistry 36, 1349-1361.
    • (1997) Biochemistry , vol.36 , pp. 1349-1361
    • Taylor, K.L.1    Xiang, H.2    Liu, R.-Q.3    Yang, G.4    Dunaway-Mariano, D.5
  • 36
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaacs, N. & Bailey, S., eds, SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Data Collection and Processing. Proceedings of the CCP4 Study Weekend. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Data Collection and Processing. Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 38
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • Wolf, W., Evans, P.R. & Leslie, A.G.W., eds, SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1991). Maximum likelihood refinement of heavy atom parameters. In Proceedings of the CCP4 Study Weekend. (Wolf, W., Evans, P.R. & Leslie, A.G.W., eds), pp. 80-85, SERC Daresbury Laboratory, Warrington, UK.
    • (1991) Proceedings of the CCP4 Study Weekend , pp. 80-85
    • Otwinowski, Z.1
  • 39
    • 0027678620 scopus 로고
    • REPLACE, a suite of computer programs for molecular-replacement calculations
    • Tong, L. (1993). REPLACE, a suite of computer programs for molecular-replacement calculations. J. Appl. Cryst. 26, 748-751.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 748-751
    • Tong, L.1
  • 40
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modification calculations
    • Cowtan, K.D. & Main, P. (1996). Phase combination and cross validation in iterated density-modification calculations. Acta Cryst. D 52, 43-48.
    • (1996) Acta Cryst. D , vol.52 , pp. 43-48
    • Cowtan, K.D.1    Main, P.2
  • 41
    • 84889120137 scopus 로고
    • Improved methods for building 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. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. & Dodson, E.J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D 53, 240-255.
    • (1997) Acta Cryst. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 44
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Cryst. D 49, 129-147.
    • (1993) Acta Cryst. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 45
    • 0002087304 scopus 로고
    • 3D search and research using the Cambridge Structural Database
    • Allen, F.H. & Kennard, O. (1993). 3D search and research using the Cambridge Structural Database. Chem. Design Automation News 8, 1 & 31-37.
    • (1993) Chem. Design Automation News , vol.8 , pp. 1
    • Allen, F.H.1    Kennard, O.2
  • 46
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 47
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. (1990). WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 48
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. & Higgins, D.G. (1997). The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 49
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly, M.L. (1993). The molecular surface package. J. Mol. Graph. 11, 139-141.
    • (1993) J. Mol. Graph. , vol.11 , pp. 139-141
    • Connolly, M.L.1
  • 50
    • 0026519169 scopus 로고
    • Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase
    • Wierenga, R.K., Noble, M.E.M. & Davenport, R.C. (1992). Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J. Mol. Biol. 224, 1115-1126.
    • (1992) J. Mol. Biol. , vol.224 , pp. 1115-1126
    • Wierenga, R.K.1    Noble, M.E.M.2    Davenport, R.C.3
  • 51
    • 0000400122 scopus 로고
    • Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 Å resolution
    • Noble, M.E.M., Zeelen, J.P. & Wierenga, R.K. (1993). Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 Å resolution. Acta Cryst. D 49, 403-417.
    • (1993) Acta Cryst. D , vol.49 , pp. 403-417
    • Noble, M.E.M.1    Zeelen, J.P.2    Wierenga, R.K.3
  • 52
    • 0028785003 scopus 로고
    • Changing stereochemistry for a metabolic pathway in vivo: Experiments with peroxismal β-oxidation
    • Filppula, S.A., Sormanen, R.T., Hartig, A., Kunau, W.-H. & Hiltunen, J.K. (1995). Changing stereochemistry for a metabolic pathway in vivo: Experiments with peroxismal β-oxidation. J. Biol. Chem. 270, 27453-27457.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27453-27457
    • Filppula, S.A.1    Sormanen, R.T.2    Hartig, A.3    Kunau, W.-H.4    Hiltunen, J.K.5
  • 53
    • 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. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 54
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt, E.A. & Bacon, D.J. (1997). Raster3D photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.