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Volumn 129, Issue 1, 2007, Pages 131-139

Understanding oligomerization in 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni: An in silico approach and evidence for an active protein

Author keywords

3 HSD CR; Dimerization; MD simulation; SDR

Indexed keywords

BACTERIA; BIOREMEDIATION; ENZYME KINETICS; MOLECULAR DYNAMICS; PROTEINS; REDOX REACTIONS; TOXIC MATERIALS;

EID: 33847011071     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.11.024     Document Type: Article
Times cited : (13)

References (25)
  • 1
    • 0031573526 scopus 로고    scopus 로고
    • The 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters
    • Auerbach G., Herrmann A., Gutlich M., Fischer M., Jacob U., Bacher A., and Huber R. The 1.25 A crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters. Embo. J. 16 (1997) 7219-7230
    • (1997) Embo. J. , vol.16 , pp. 7219-7230
    • Auerbach, G.1    Herrmann, A.2    Gutlich, M.3    Fischer, M.4    Jacob, U.5    Bacher, A.6    Huber, R.7
  • 2
    • 0032544367 scopus 로고    scopus 로고
    • The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution
    • Benach J., Atrian S., Gonzalez-Duarte R., and Ladenstein R. The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution. J. Mol. Biol. 282 (1998) 383-399
    • (1998) J. Mol. Biol. , vol.282 , pp. 383-399
    • Benach, J.1    Atrian, S.2    Gonzalez-Duarte, R.3    Ladenstein, R.4
  • 3
    • 0033523083 scopus 로고    scopus 로고
    • The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography
    • Benach J., Atrian S., Gonzalez-Duarte R., and Ladenstein R. The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography. J. Mol. Biol. 289 (1999) 335-355
    • (1999) J. Mol. Biol. , vol.289 , pp. 335-355
    • Benach, J.1    Atrian, S.2    Gonzalez-Duarte, R.3    Ladenstein, R.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 33846823909 scopus 로고
    • Particle mesh Ewald-An N.log(N) method for Ewald sums in large systems
    • Darden T., York D., and Pedersen L. Particle mesh Ewald-An N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98 (1993) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 8
    • 0028773893 scopus 로고
    • The refined three-dimensional structure of 3 alpha, 20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases
    • Ghosh D., Wawrzak Z., Weeks C.M., Duax W.L., and Erman M. The refined three-dimensional structure of 3 alpha, 20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases. Structure 2 (1994) 629-640
    • (1994) Structure , vol.2 , pp. 629-640
    • Ghosh, D.1    Wawrzak, Z.2    Weeks, C.M.3    Duax, W.L.4    Erman, M.5
  • 9
    • 0034731149 scopus 로고    scopus 로고
    • The crystal structure of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family
    • Grimm C., Maser E., Möbus E., Klebe G., Reuter K., and Ficner R. The crystal structure of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni shows a novel oligomerization pattern within the short chain dehydrogenase/reductase family. J. Biol. Chem. 275 (2000) 41333-41339
    • (2000) J. Biol. Chem. , vol.275 , pp. 41333-41339
    • Grimm, C.1    Maser, E.2    Möbus, E.3    Klebe, G.4    Reuter, K.5    Ficner, R.6
  • 10
    • 33947172229 scopus 로고    scopus 로고
    • Structural aspects of oligomerization in 3alpha-hydroxysteroid dehydrogenase from Comamonas testosteroni: redesign of an "extraloop"-domain on the basis of 3alpha/20beta-HSD. Vol. Genes, Gene Families, and Isozymes Bologna
    • Hoffmann F., Xiong G., Sotriffer C., Reuter K., and Maser E. Structural aspects of oligomerization in 3alpha-hydroxysteroid dehydrogenase from Comamonas testosteroni: redesign of an "extraloop"-domain on the basis of 3alpha/20beta-HSD. Vol. Genes, Gene Families, and Isozymes Bologna. Medimond (2003) 123-132
    • (2003) Medimond , pp. 123-132
    • Hoffmann, F.1    Xiong, G.2    Sotriffer, C.3    Reuter, K.4    Maser, E.5
  • 12
    • 0027241460 scopus 로고
    • Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl reductase)
    • Krook M., Ghosh D., Duax W., and Jörnvall H. Three-dimensional model of NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase and relationships to the NADP(+)-dependent enzyme (carbonyl reductase). FEBS Lett. 322 (1993) 139-142
    • (1993) FEBS Lett. , vol.322 , pp. 139-142
    • Krook, M.1    Ghosh, D.2    Duax, W.3    Jörnvall, H.4
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0033642945 scopus 로고    scopus 로고
    • Structural stability of binding sites: consequences for binding affinity and allosteric effects.
    • Luque I., and Freire E. Structural stability of binding sites: consequences for binding affinity and allosteric effects. Proteins 4 Suppl. (2000) 63-71
    • (2000) Proteins , vol.4 , Issue.SUPPL , pp. 63-71
    • Luque, I.1    Freire, E.2
  • 15
    • 0000068909 scopus 로고
    • Induction and purification of alpha- and beta-hydroxysteroid dehydrogenases
    • Marcus P.I., and Talalay P. Induction and purification of alpha- and beta-hydroxysteroid dehydrogenases. J. Biol. Chem. 218 (1956) 661-674
    • (1956) J. Biol. Chem. , vol.218 , pp. 661-674
    • Marcus, P.I.1    Talalay, P.2
  • 16
    • 0343090874 scopus 로고    scopus 로고
    • Functional expression, purification, and characterization of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni
    • Maser E., Möbus E., and Xiong G. Functional expression, purification, and characterization of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. Biochem. Biophys. Res. Commun. 272 (2000) 622-628
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 622-628
    • Maser, E.1    Möbus, E.2    Xiong, G.3
  • 17
    • 0030955228 scopus 로고    scopus 로고
    • Testosterone-regulated expression of enzymes involved in steroid and aromatic hydrocarbon catabolism in Comamonas testosteroni
    • Möbus E., Jahn M., Schmid R., Jahn D., and Maser E. Testosterone-regulated expression of enzymes involved in steroid and aromatic hydrocarbon catabolism in Comamonas testosteroni. J. Bacteriol. 179 (1997) 5951-5955
    • (1997) J. Bacteriol. , vol.179 , pp. 5951-5955
    • Möbus, E.1    Jahn, M.2    Schmid, R.3    Jahn, D.4    Maser, E.5
  • 18
    • 0032553317 scopus 로고    scopus 로고
    • Molecular cloning, overexpression, and characterization of steroid-inducible 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily
    • Möbus E., and Maser E. Molecular cloning, overexpression, and characterization of steroid-inducible 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. A novel member of the short-chain dehydrogenase/reductase superfamily. J. Biol. Chem. 273 (1998) 30888-30896
    • (1998) J. Biol. Chem. , vol.273 , pp. 30888-30896
    • Möbus, E.1    Maser, E.2
  • 19
    • 0030152146 scopus 로고    scopus 로고
    • Antibiotic resistance and enhanced insecticide catabolism as consequences of steroid induction in the gram-negative bacterium Comamonas testosteroni
    • Oppermann U.C., Belai I., and Maser E. Antibiotic resistance and enhanced insecticide catabolism as consequences of steroid induction in the gram-negative bacterium Comamonas testosteroni. J. Steroid. Biochem. Mol. Biol. 58 (1996) 217-223
    • (1996) J. Steroid. Biochem. Mol. Biol. , vol.58 , pp. 217-223
    • Oppermann, U.C.1    Belai, I.2    Maser, E.3
  • 20
  • 21
    • 33947119904 scopus 로고    scopus 로고
    • Rossmann, M.G., Liljas, A., Bränden, C.I., Banaszal, L.J., 1975. The Enzymes, pp. 61-102.
  • 22
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 23
    • 0029643855 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
    • Tanaka N., Nonaka T., Nakanishi M., Deyashiki Y., Hara A., and Mitsui Y. Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure 4 (1996) 33-45
    • (1996) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6
  • 25
    • 0033607498 scopus 로고    scopus 로고
    • The catalytic triad in Drosophila alcohol dehydrogenase: pH, temperature and molecular modelling studies
    • Winberg J.O., Brendskag M.K., Sylte I., Lindstad R.I., and McKinley-McKee J.S. The catalytic triad in Drosophila alcohol dehydrogenase: pH, temperature and molecular modelling studies. J. Mol. Biol. 294 (1999) 601-616
    • (1999) J. Mol. Biol. , vol.294 , pp. 601-616
    • Winberg, J.O.1    Brendskag, M.K.2    Sylte, I.3    Lindstad, R.I.4    McKinley-McKee, J.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.