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Volumn 16, Issue 12, 2007, Pages 2647-2656

Distortion of flavin geometry is linked to ligand binding in cholesterol oxidase

Author keywords

Cholesterol oxidase; Flavin; Flavin activation; Michaelis complex; Redox potential

Indexed keywords

AROMATIC COMPOUND; BACTERIAL ENZYME; CHOLESTEROL OXIDASE; FLAVINE ADENINE NUCLEOTIDE; GLYCEROL; QUERCETIN;

EID: 36448940092     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073168207     Document Type: Article
Times cited : (25)

References (34)
  • 2
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Cryst. D 50: 760-763.
    • Collaborative Computational Project, Number4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Cryst. D 50: 760-763.
  • 3
    • 0035839498 scopus 로고    scopus 로고
    • Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair
    • Coulombe, R., Yue, K.Q., Ghisla, S., and Vrielink, A. 2001. Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair. J. Biol. Chem. 276: 30435-30441.
    • (2001) J. Biol. Chem , vol.276 , pp. 30435-30441
    • Coulombe, R.1    Yue, K.Q.2    Ghisla, S.3    Vrielink, A.4
  • 4
    • 0001490107 scopus 로고
    • Electron paramagnetic resonance study of the mixed-valent diiron center in Escherichia coli ribonucleotide reductase produced by reduction of radical-free protein R2 at 77 K
    • Davydov, R., Kuprin, S., Gräslund, A., and Ehrenberg, A. 1994. Electron paramagnetic resonance study of the mixed-valent diiron center in Escherichia coli ribonucleotide reductase produced by reduction of radical-free protein R2 at 77 K. J. Am. Chem. Soc. 116: 11120-11128.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 11120-11128
    • Davydov, R.1    Kuprin, S.2    Gräslund, A.3    Ehrenberg, A.4
  • 5
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. 2004. Coot: Model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60: 2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 6
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • Fraaije, M.W. and Mattevi, A. 2000. Flavoenzymes: Diverse catalysts with recurrent features. Trends Biochem. Sci. 25: 126-132.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 7
    • 0023658602 scopus 로고
    • Further consideration of flavin coenzyme biochemistry afforded by geometry-optimized molecular orbital calculations
    • Hall, L.H., Bowers, M.L., and Durfor, C.N. 1987. Further consideration of flavin coenzyme biochemistry afforded by geometry-optimized molecular orbital calculations. Biochemistry 26: 7401-7409.
    • (1987) Biochemistry , vol.26 , pp. 7401-7409
    • Hall, L.H.1    Bowers, M.L.2    Durfor, C.N.3
  • 8
    • 0000275732 scopus 로고    scopus 로고
    • Conformational effects on flavin redox chemistry
    • Hasford, J.K., Kemnitzer, W., and Rizzo, C.J. 1997. Conformational effects on flavin redox chemistry. J. Org. Chem. 62: 5244-5245.
    • (1997) J. Org. Chem , vol.62 , pp. 5244-5245
    • Hasford, J.K.1    Kemnitzer, W.2    Rizzo, C.J.3
  • 9
    • 0030856396 scopus 로고    scopus 로고
    • Pathogenesis and virulence of Rhodococcus equi
    • Hondalus, M.K. 1997. Pathogenesis and virulence of Rhodococcus equi. Vet. Microbiol. 56: 257-268.
    • (1997) Vet. Microbiol , vol.56 , pp. 257-268
    • Hondalus, M.K.1
  • 10
    • 0032491078 scopus 로고    scopus 로고
    • 361 position in the reaction catalyzed by cholesterol oxidase
    • 361 position in the reaction catalyzed by cholesterol oxidase. Bioorg. Med. Chem. Lett. 8: 2663-2668.
    • (1998) Bioorg. Med. Chem. Lett , vol.8 , pp. 2663-2668
    • Kass, I.J.1    Sampson, N.S.2
  • 11
    • 0032558937 scopus 로고    scopus 로고
    • Evaluation of the role of His447 in the reaction catalyzed by cholesterol oxidase
    • Kass, I.J. and Sampson, N.S. 1998b. Evaluation of the role of His447 in the reaction catalyzed by cholesterol oxidase. Biochemistry 37: 17990-18000.
    • (1998) Biochemistry , vol.37 , pp. 17990-18000
    • Kass, I.J.1    Sampson, N.S.2
  • 12
    • 0037424631 scopus 로고    scopus 로고
    • Sub-atomic resolution crystal structure of cholesterol oxidase: What atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity
    • Lario, P.I., Sampson, N., and Vrielink, A. 2003. Sub-atomic resolution crystal structure of cholesterol oxidase: What atomic resolution crystallography reveals about enzyme mechanism and the role of the FAD cofactor in redox activity. J. Mol. Biol. 326: 1635-1650.
    • (2003) J. Mol. Biol , vol.326 , pp. 1635-1650
    • Lario, P.I.1    Sampson, N.2    Vrielink, A.3
  • 13
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and 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
  • 14
    • 0032725979 scopus 로고    scopus 로고
    • Crystal structure of reduced thioredoxin reductase from Escherichia coli: Structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor
    • Lennon, B.W., Williams Jr., C.H., and Ludwig, M.L. 1999. Crystal structure of reduced thioredoxin reductase from Escherichia coli: Structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor. Protein Sci. 8: 2366-2379.
    • (1999) Protein Sci , vol.8 , pp. 2366-2379
    • Lennon, B.W.1    Williams Jr., C.H.2    Ludwig, M.L.3
  • 15
    • 0027432601 scopus 로고
    • Crystal structure of cholesterol oxidase complexed with a steroid substrate: Implications for flavin adenine dinucleotide dependent alcohol oxidases
    • Li, J., Vrielink, A., Brick, P., and Blow, D.M. 1993. Crystal structure of cholesterol oxidase complexed with a steroid substrate: Implications for flavin adenine dinucleotide dependent alcohol oxidases. Biochemistry 32: 11507-11515.
    • (1993) Biochemistry , vol.32 , pp. 11507-11515
    • Li, J.1    Vrielink, A.2    Brick, P.3    Blow, D.M.4
  • 16
    • 33751103925 scopus 로고    scopus 로고
    • Structural and kinetic analyses of the H121A mutant of cholesterol oxidase
    • Lim, L., Molla, G., Guinn, N., Ghisla, S., Pollegioni, L., and Vrielink, A. 2006. Structural and kinetic analyses of the H121A mutant of cholesterol oxidase. Biochem. J. 400: 13-22.
    • (2006) Biochem. J , vol.400 , pp. 13-22
    • Lim, L.1    Molla, G.2    Guinn, N.3    Ghisla, S.4    Pollegioni, L.5    Vrielink, A.6
  • 17
    • 0030756006 scopus 로고    scopus 로고
    • Oxidation of macrophage membrane cholesterol by intracellular Rhodococcus equi
    • Linder, R. and Bernheimer, A.W. 1997. Oxidation of macrophage membrane cholesterol by intracellular Rhodococcus equi. Vet. Microbiol. 56: 269-276.
    • (1997) Vet. Microbiol , vol.56 , pp. 269-276
    • Linder, R.1    Bernheimer, A.W.2
  • 19
    • 0036850805 scopus 로고    scopus 로고
    • Physical and chemical considerations of damage induced in protein crystals by synchrotron radiation: A radiation chemical perspective
    • O'Neill, P., Stevens, D.L., and Garman, E.F. 2002. Physical and chemical considerations of damage induced in protein crystals by synchrotron radiation: A radiation chemical perspective. J. Synchrotron Radiat. 9: 329-332.
    • (2002) J. Synchrotron Radiat , vol.9 , pp. 329-332
    • O'Neill, P.1    Stevens, D.L.2    Garman, E.F.3
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. 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
  • 21
    • 33750975092 scopus 로고    scopus 로고
    • Cholesterol oxidase (ChoE) is not important in the virulence of Rhodococcus equi
    • Pei, Y., Dupont, C., Sydor, T., Haas, A., and Prescott, J.F. 2006. Cholesterol oxidase (ChoE) is not important in the virulence of Rhodococcus equi. Vet. Microbiol. 118: 240-246.
    • (2006) Vet. Microbiol , vol.118 , pp. 240-246
    • Pei, Y.1    Dupont, C.2    Sydor, T.3    Haas, A.4    Prescott, J.F.5
  • 22
    • 85061917866 scopus 로고    scopus 로고
    • Potentiometric measurements of proteins
    • eds. A.J. Bard and M. Stratmann, pp, Wiley, VCH, Weinheim, Germany
    • Pellett, J. and Stankovich, M. 2002. Potentiometric measurements of proteins. In Encyclopedia electrochemistry. (eds. A.J. Bard and M. Stratmann), pp. 485-509. Wiley, VCH, Weinheim, Germany.
    • (2002) Encyclopedia electrochemistry , pp. 485-509
    • Pellett, J.1    Stankovich, M.2
  • 23
    • 0033213239 scopus 로고    scopus 로고
    • The finer things in X-ray diffraction data collection
    • Pflugrath, J.W. 1999. The finer things in X-ray diffraction data collection. Acta Crystallogr. D Biol. Crystallogr. 55: 1718-1725.
    • (1999) Acta Crystallogr. D Biol. Crystallogr , vol.55 , pp. 1718-1725
    • Pflugrath, J.W.1
  • 24
    • 0034611517 scopus 로고    scopus 로고
    • X-ray crystal structures of conformationally biased flavin models
    • Reibenspies, J.H., Guo, F., and Rizzo, C.J. 2000. X-ray crystal structures of conformationally biased flavin models. Org. Lett. 2: 903-906.
    • (2000) Org. Lett , vol.2 , pp. 903-906
    • Reibenspies, J.H.1    Guo, F.2    Rizzo, C.J.3
  • 25
    • 0141431067 scopus 로고    scopus 로고
    • Cholesterol oxidases: A study of nature's approach to protein design
    • Sampson, N.S. and Vrielink, A. 2003. Cholesterol oxidases: A study of nature's approach to protein design. Acc. Chem. Res. 36: 713-722.
    • (2003) Acc. Chem. Res , vol.36 , pp. 713-722
    • Sampson, N.S.1    Vrielink, A.2
  • 26
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • eds. C.W.J. Carter Jr. and R.M. Sweet, pp, Academic Press, Orlando, FL
    • Sheldrick, G.M. and Schneider, T.R. 1997. SHELXL: High-resolution refinement. In Methods in enzymology (eds. C.W.J. Carter Jr. and R.M. Sweet), pp. 319-343. Academic Press, Orlando, FL.
    • (1997) Methods in enzymology , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 28
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine, A.A., Richelle, J., and Wodak, S.J. 1999. SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr. D Biol. Crystallogr. 55: 191-205.
    • (1999) Acta Crystallogr. D Biol. Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 29
    • 0025793579 scopus 로고
    • Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution
    • Vrielink, A., Lloyd, L.F., and Blow, D.M. 1991. Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution. J. Mol. Biol. 219: 533-554.
    • (1991) J. Mol. Biol , vol.219 , pp. 533-554
    • Vrielink, A.1    Lloyd, L.F.2    Blow, D.M.3
  • 30
    • 0037418636 scopus 로고    scopus 로고
    • Flavin reduction potential tuning by substitution and bending
    • Walsh, J.D. and Miller, A.-F. 2003. Flavin reduction potential tuning by substitution and bending. J. Mol. Struct. 623: 185-195.
    • (2003) J. Mol. Struct , vol.623 , pp. 185-195
    • Walsh, J.D.1    Miller, A.-F.2
  • 31
    • 33646446575 scopus 로고    scopus 로고
    • Functional studies to probe the active site structure of cholesterol oxidase
    • Ph.D thesis, State University of New York, Stony Brook, NY
    • Yin, Y. 2002. "Functional studies to probe the active site structure of cholesterol oxidase." Ph.D thesis, State University of New York, Stony Brook, NY.
    • (2002)
    • Yin, Y.1
  • 32
    • 0035923397 scopus 로고    scopus 로고
    • The presence of a hydrogen bond between asparagine 485 and the pi system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase
    • Yin, Y., Sampson, N.S., Vrielink, A., and Lario, P.I. 2001. The presence of a hydrogen bond between asparagine 485 and the pi system of FAD modulates the redox potential in the reaction catalyzed by cholesterol oxidase. Biochemistry 40: 13779-13787.
    • (2001) Biochemistry , vol.40 , pp. 13779-13787
    • Yin, Y.1    Sampson, N.S.2    Vrielink, A.3    Lario, P.I.4
  • 33
    • 0037098498 scopus 로고    scopus 로고
    • Construction of a catalytically inactive cholesterol oxidase mutant: Investigation of the interplay between active site-residues glutamate 361 and histidine 447
    • Yin, Y., Liu, P., Anderson, R.G., and Sampson, N.S. 2002. Construction of a catalytically inactive cholesterol oxidase mutant: Investigation of the interplay between active site-residues glutamate 361 and histidine 447. Arch. Biochem. Biophys. 402: 235-242.
    • (2002) Arch. Biochem. Biophys , vol.402 , pp. 235-242
    • Yin, Y.1    Liu, P.2    Anderson, R.G.3    Sampson, N.S.4
  • 34
    • 0033528745 scopus 로고    scopus 로고
    • Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants
    • Yue, Q.K., Kass, I.J., Sampson, N.S., and Vrielink, A. 1999. Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants. Biochemistry 38: 4277-4286.
    • (1999) Biochemistry , vol.38 , pp. 4277-4286
    • Yue, Q.K.1    Kass, I.J.2    Sampson, N.S.3    Vrielink, A.4


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