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Volumn 288, Issue 36, 2013, Pages 26235-26245

Crystal structure of 3-hydroxybenzoate 6-hydroxylase uncovers lipid-assisted flavoprotein strategy for regioselective aromatic hydroxylation

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC HYDROXYLATION; BOUND LIPIDS; MONOOXYGENASES; REGIO-SELECTIVE; SOIL MICRO-ORGANISMS; STRUCTURE FEATURES; SUBSTRATE BINDING; SUBSTRATE-BINDING SITES;

EID: 84883693290     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.479303     Document Type: Article
Times cited : (45)

References (53)
  • 1
    • 80052794668 scopus 로고    scopus 로고
    • Catalytic and structural features of flavoprotein hydroxylases and epoxidases
    • Montersino, S., Tischler, D., Gassner, G. T., and van Berkel, W. J. (2011) Catalytic and structural features of flavoprotein hydroxylases and epoxidases. Adv. Synth. Catal. 353, 2301-2319
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2301-2319
    • Montersino, S.1    Tischler, D.2    Gassner, G.T.3    Van Berkel, W.J.4
  • 2
    • 33745991798 scopus 로고    scopus 로고
    • Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
    • van Berkel, W. J., Kamerbeek, N. M., and Fraaije, M. W. (2006) Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J. Biotechnol. 124, 670-689
    • (2006) J. Biotechnol. , vol.124 , pp. 670-689
    • Van Berkel, W.J.1    Kamerbeek, N.M.2    Fraaije, M.W.3
  • 3
    • 72049124811 scopus 로고    scopus 로고
    • Control of catalysis in flavin-dependent monooxygenases
    • Palfey, B. A., and McDonald, C. A. (2010) Control of catalysis in flavin-dependent monooxygenases. Arch. Biochem. Biophys. 493, 26-36
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 26-36
    • Palfey, B.A.1    McDonald, C.A.2
  • 4
    • 0024974962 scopus 로고
    • Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution Analysis of the enzyme-substrate and enzyme-product complexes
    • Schreuder, H. A., Prick, P. A., Wierenga, R. K., Vriend, G., Wilson, K. S., Hol, W. G., and Drenth, J. (1989) Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes. J. Mol. Biol. 208, 679-696
    • (1989) J. Mol. Biol. , vol.208 , pp. 679-696
    • Schreuder, H.A.1    Prick, P.A.2    Wierenga, R.K.3    Vriend, G.4    Wilson, K.S.5    Hol, W.G.6    Drenth, J.7
  • 5
    • 0032524753 scopus 로고    scopus 로고
    • The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
    • Enroth, C., Neujahr, H., Schneider, G., and Lindqvist, Y. (1998) The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis. Structure 6, 605-617
    • (1998) Structure , vol.6 , pp. 605-617
    • Enroth, C.1    Neujahr, H.2    Schneider, G.3    Lindqvist, Y.4
  • 6
    • 33751105570 scopus 로고    scopus 로고
    • Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site
    • Hiromoto, T., Fujiwara, S., Hosokawa, K., and Yamaguchi, H. (2006) Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site. J. Mol. Biol. 364, 878-896
    • (2006) J. Mol. Biol. , vol.364 , pp. 878-896
    • Hiromoto, T.1    Fujiwara, S.2    Hosokawa, K.3    Yamaguchi, H.4
  • 7
    • 66049102551 scopus 로고    scopus 로고
    • Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5- carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications
    • McCulloch, K. M., Mukherjee, T., Begley, T. P., and Ealick, S. E. (2009) Structure of the PLP degradative enzyme 2-methyl-3-hydroxypyridine-5- carboxylic acid oxygenase from Mesorhizobium loti MAFF303099 and its mechanistic implications. Biochemistry 48, 4139-4149
    • (2009) Biochemistry , vol.48 , pp. 4139-4149
    • McCulloch, K.M.1    Mukherjee, T.2    Begley, T.P.3    Ealick, S.E.4
  • 8
    • 42749083544 scopus 로고    scopus 로고
    • Structure of 2,6-dihydroxypyridine 3-hydroxylase from a nicotine-degrading pathway
    • Treiber, N., and Schulz, G. E. (2008) Structure of 2,6-dihydroxypyridine 3-hydroxylase from a nicotine-degrading pathway. J. Mol. Biol. 379, 94-104
    • (2008) J. Mol. Biol. , vol.379 , pp. 94-104
    • Treiber, N.1    Schulz, G.E.2
  • 13
    • 79953250020 scopus 로고    scopus 로고
    • Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase
    • Volkers, G., Palm, G. J., Weiss, M. S., Wright, G. D., and Hinrichs, W. (2011) Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase. FEBS Lett. 585, 1061-1066
    • (2011) FEBS Lett. , vol.585 , pp. 1061-1066
    • Volkers, G.1    Palm, G.J.2    Weiss, M.S.3    Wright, G.D.4    Hinrichs, W.5
  • 14
    • 84856058506 scopus 로고    scopus 로고
    • Functional annotation and characterization of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1
    • Montersino, S., and van Berkel, W. J. (2012) Functional annotation and characterization of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1. Biochim. Biophys. Acta 1824, 433-442
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 433-442
    • Montersino, S.1    Van Berkel, W.J.2
  • 16
    • 0026715272 scopus 로고
    • The biology and genetics of the genus Rhodococcus
    • Finnerty, W. R. (1992) The biology and genetics of the genus Rhodococcus. Annu. Rev. Microbiol. 46, 193-218
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 193-218
    • Finnerty, W.R.1
  • 17
    • 2642561830 scopus 로고    scopus 로고
    • Can whole genome analysis refine the taxonomy of the genus Rhodococcus? FEMS Microbiol
    • Gürtler, V., Mayall, B. C., and Seviour, R. (2004) Can whole genome analysis refine the taxonomy of the genus Rhodococcus? FEMS Microbiol. Rev. 28, 377-403
    • (2004) Rev. , vol.28 , pp. 377-403
    • Gürtler, V.1    Mayall, B.C.2    Seviour, R.3
  • 18
    • 2942529079 scopus 로고    scopus 로고
    • Harnessing the catabolic diversity of rhodococci for environmental and biotechnological applications
    • van der Geize, R., and Dijkhuizen, L. (2004) Harnessing the catabolic diversity of rhodococci for environmental and biotechnological applications. Curr. Opin. Microbiol. 7, 255-261
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 255-261
    • Van Der Geize, R.1    Dijkhuizen, L.2
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 22
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E: Combining chain tracing with density modification
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E: combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 479-485
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 23
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for x-ray crystallography using ARP/ wARP version
    • Langer, G., Cohen, S. X., Lamzin, V. S., and Perrakis, A. (2008) Automated macromolecular model building for x-ray crystallography using ARP/ wARP version Nat. Protoc. 3, 1171-1179
    • (2008) Nat. Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 28
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus, P. A., and Diederichs, K. (2012) Linking crystallographic model and data quality. Science 336, 1030-1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 29
    • 0030716522 scopus 로고    scopus 로고
    • Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding
    • Eppink, M. H., Schreuder, H. A., and van Berkel, W. J. (1997) Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding. Protein Sci. 6, 2454-2458
    • (1997) Protein Sci. , vol.6 , pp. 2454-2458
    • Eppink, M.H.1    Schreuder, H.A.2    Van Berkel, W.J.3
  • 30
    • 9744270010 scopus 로고    scopus 로고
    • Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase
    • Entsch, B., Cole, L. J., and Ballou, D. P. (2005) Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase. Arch. Biochem. Biophys. 433, 297-311
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 297-311
    • Entsch, B.1    Cole, L.J.2    Ballou, D.P.3
  • 31
    • 0029001789 scopus 로고
    • Structure and mechanism of parahydroxybenzoate hydroxylase
    • Entsch, B., and van Berkel, W. J. (1995) Structure and mechanism of parahydroxybenzoate hydroxylase. FASEB J. 9, 476-483
    • (1995) FASEB J. , vol.9 , pp. 476-483
    • Entsch, B.1    Van Berkel, W.J.2
  • 32
    • 0032516920 scopus 로고    scopus 로고
    • Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants
    • Eppink, M. H., Schreuder, H. A., and van Berkel, W. J. (1998) Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, crystallographic and modeling studies of histidine 162 and arginine 269 variants. J. Biol. Chem. 273, 21031-21039
    • (1998) J. Biol. Chem. , vol.273 , pp. 21031-21039
    • Eppink, M.H.1    Schreuder, H.A.2    Van Berkel, W.J.3
  • 35
    • 80052785784 scopus 로고    scopus 로고
    • (Frago, S., Gomez-Moreno, C., and Medina, M., eds) Prensas Universitarias de Zaragoza, Zaragoza, Spain
    • Montersino, S., Golovleva, L., Schlömann, M., and van Berkel, W. J. H. (2008) in Flavins and Flavoproteins (Frago, S., Gomez-Moreno, C., and Medina, M., eds) pp. 51-56, Prensas Universitarias de Zaragoza, Zaragoza, Spain
    • (2008) Flavins and Flavoproteins , pp. 51-56
    • Montersino, S.1    Golovleva, L.2    Schlömann, M.3    Van Berkel, W.J.H.4
  • 36
    • 0020775064 scopus 로고
    • P-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens Fitting of the amino-acid sequence to the tertiary structure
    • Weijer, W. J., Hofsteenge, J., Beintema, J. J., Wierenga, R. K., and Drenth, J. (1983) p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens Fitting of the amino-acid sequence to the tertiary structure. Eur. J. Biochem. 133, 109-118
    • (1983) Eur. J. Biochem , vol.133 , pp. 109-118
    • Weijer, W.J.1    Hofsteenge, J.2    Beintema, J.J.3    Wierenga, R.K.4    Drenth, J.5
  • 39
    • 34249722165 scopus 로고    scopus 로고
    • Lipid composition of membranes of Escherichia coli by liquid chromatography/tandem mass spectrometry using negative electrospray ionization
    • Oursel, D., Loutelier-Bourhis, C., Orange, N., Chevalier, S., Norris, V., and Lange, C. M. (2007) Lipid composition of membranes of Escherichia coli by liquid chromatography/tandem mass spectrometry using negative electrospray ionization. Rapid Commun. Mass Spectrom. 21, 1721-1728
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 1721-1728
    • Oursel, D.1    Loutelier-Bourhis, C.2    Orange, N.3    Chevalier, S.4    Norris, V.5    Lange, C.M.6
  • 40
    • 0141974064 scopus 로고    scopus 로고
    • Electrospray mass spectrometry of phospholipids
    • Pulfer, M., and Murphy, R. C. (2003) Electrospray mass spectrometry of phospholipids. Mass Spectrom. Rev. 22, 332-364
    • (2003) Mass Spectrom. Rev. , vol.22 , pp. 332-364
    • Pulfer, M.1    Murphy, R.C.2
  • 42
    • 0025925008 scopus 로고
    • Purification and char- acterisation of 3-hydroxyphenylacetate 6-hydroxylase: A novel FAD-dependent monooxygenase from a Flavobacterium species
    • Van Berkel, W. J., and Van Den Tweel, W. J. (1991) Purification and char- acterisation of 3-hydroxyphenylacetate 6-hydroxylase: a novel FAD-dependent monooxygenase from a Flavobacterium species. Eur. J. Biochem. 201, 585-592
    • (1991) Eur. J. Biochem. , vol.201 , pp. 585-592
    • Van Berkel, W.J.1    Van Den Tweel, W.J.2
  • 43
    • 0015902864 scopus 로고
    • On the interaction of para-hydroxybenzoate hydroxylase from Pseudomonas fluorescens with halogen ions
    • Steennis, P. J., Cordes, M. M., Hilkens, J. H., and Müller, F. (1973) On the interaction of para-hydroxybenzoate hydroxylase from Pseudomonas fluorescens with halogen ions. FEBS Lett. 36, 177-180
    • (1973) FEBS Lett. , vol.36 , pp. 177-180
    • Steennis, P.J.1    Cordes, M.M.2    Hilkens, J.H.3    Müller, F.4
  • 46
    • 80053164218 scopus 로고    scopus 로고
    • Coq6 hydroxylase: Unmasked and bypassed
    • Clarke, C. F. (2011) Coq6 hydroxylase: unmasked and bypassed. Chem. Biol. 18, 1069-1070
    • (2011) Chem. Biol. , vol.18 , pp. 1069-1070
    • Clarke, C.F.1
  • 47
    • 80053160231 scopus 로고    scopus 로고
    • Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency
    • Ozeir, M., Mühlenhoff, U., Webert, H., Lill, R., Fontecave, M., and Pierrel, F. (2011) Coenzyme Q biosynthesis: Coq6 is required for the C5-hydroxylation reaction and substrate analogs rescue Coq6 deficiency. Chem. Biol. 18, 1134-1142
    • (2011) Chem. Biol. , vol.18 , pp. 1134-1142
    • Ozeir, M.1    Mühlenhoff, U.2    Webert, H.3    Lill, R.4    Fontecave, M.5    Pierrel, F.6
  • 48
    • 0034607970 scopus 로고    scopus 로고
    • Ubiquinone (coenzyme Q) biosynthesis in Escherichia coli: Identification of the ubiF gene
    • Kwon, O., Kotsakis, A., and Meganathan, R. (2000) Ubiquinone (coenzyme Q) biosynthesis in Escherichia coli: identification of the ubiF gene. FEMS Microbiol. Lett. 186, 157-161
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 157-161
    • Kwon, O.1    Kotsakis, A.2    Meganathan, R.3
  • 49
    • 0035949539 scopus 로고    scopus 로고
    • Ubiquinone biosynthesis in microorganisms
    • Meganathan, R. (2001) Ubiquinone biosynthesis in microorganisms. FEMS Microbiol. Lett. 203, 131-139
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 131-139
    • Meganathan, R.1
  • 51
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 52
    • 0035012982 scopus 로고    scopus 로고
    • STRAP: Editor for structural alignments of proteins
    • Gille, C., and Frömmel, C. (2001) STRAP: editor for STRuctural Alignments of Proteins. Bioinformatics 17, 377-378
    • (2001) Bioinformatics , vol.17 , pp. 377-378
    • Gille, C.1    Frömmel, C.2
  • 53
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


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