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Volumn 403, Issue 2, 2010, Pages 260-269

Crystal Structure of Γ-Hexachlorocyclohexane Dehydrochlorinase LinA from Sphingobium japonicum UT26

Author keywords

Crystallography; Dehydrochlorinase; LinA; Sphingobium japonicum UT26; hexachlorocyclohexane

Indexed keywords

BACTERIAL ENZYME; DEHYDROCHLORINASE; HYDROLYASE; LINDANE; ORGANOCHLORINE DERIVATIVE; PENTACHLOROCYCLOHEXENE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DEHYDROCHLORINASES; LYASE; PROTEIN SUBUNIT;

EID: 77957232725     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.043     Document Type: Article
Times cited : (39)

References (45)
  • 1
    • 0032146829 scopus 로고    scopus 로고
    • Differential toxicity and environmental fates of hexachlorocyclohexane isomers
    • Willett K., Ulrich E., Hites R. Differential toxicity and environmental fates of hexachlorocyclohexane isomers. Environ. Sci. Technol. 1998, 32:2197-2207.
    • (1998) Environ. Sci. Technol. , vol.32 , pp. 2197-2207
    • Willett, K.1    Ulrich, E.2    Hites, R.3
  • 2
    • 0033572957 scopus 로고    scopus 로고
    • Factors influencing the distribution of lindane and other hexachlorocyclohexanes in the environment
    • Walker K. Factors influencing the distribution of lindane and other hexachlorocyclohexanes in the environment. Environ. Sci. Technol. 1999, 33:4373-4378.
    • (1999) Environ. Sci. Technol. , vol.33 , pp. 4373-4378
    • Walker, K.1
  • 3
    • 0000396578 scopus 로고
    • Dehydrochlorination of Γ-hexachlorocyclohexane (Γ-BHC) by Γ-BHC-assimilating Pseudomonas paucimobilis
    • Imai R., Nagata Y., Senoo K., Wada H., Fukuda M., Takagi M., Yano K. Dehydrochlorination of Γ-hexachlorocyclohexane (Γ-BHC) by Γ-BHC-assimilating Pseudomonas paucimobilis. Agric. Biol. Chem. 1989, 53:2015-2017.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2015-2017
    • Imai, R.1    Nagata, Y.2    Senoo, K.3    Wada, H.4    Fukuda, M.5    Takagi, M.6    Yano, K.7
  • 4
    • 1842454814 scopus 로고    scopus 로고
    • Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer
    • Dogra C., Raina V., Pal R., Suar M., Lal S., Gartemann K.H., et al. Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer. J. Bacteriol. 2004, 186:2225-2235.
    • (2004) J. Bacteriol. , vol.186 , pp. 2225-2235
    • Dogra, C.1    Raina, V.2    Pal, R.3    Suar, M.4    Lal, S.5    Gartemann, K.H.6
  • 5
    • 0025133035 scopus 로고
    • Degradation of α-, β-, and Γ-hexachlorocyclohexane by a soil bacterium under aerobic conditions
    • Sahu S.K., Patnaik K.K., Sharmila M., Sethunathan N. Degradation of α-, β-, and Γ-hexachlorocyclohexane by a soil bacterium under aerobic conditions. Appl. Environ. Microbiol. 1990, 56:3620-3622.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3620-3622
    • Sahu, S.K.1    Patnaik, K.K.2    Sharmila, M.3    Sethunathan, N.4
  • 6
    • 23944446592 scopus 로고    scopus 로고
    • 16S rDNA phylogeny and distribution of lin genes in novel hexachlorocyclohexane-degrading Sphingomonas strains
    • Böltner D., Moreno-Morillas S., Ramos J.L. 16S rDNA phylogeny and distribution of lin genes in novel hexachlorocyclohexane-degrading Sphingomonas strains. Environ. Microbiol. 2005, 7:1329-1338.
    • (2005) Environ. Microbiol. , vol.7 , pp. 1329-1338
    • Böltner, D.1    Moreno-Morillas, S.2    Ramos, J.L.3
  • 7
    • 33644960166 scopus 로고    scopus 로고
    • Distribution and phylogeny of hexachlorocyclohexane-degrading bacteria in soils from Spain
    • Mohn W.W., Mertens B., Neufeld J.D., Verstraete W., de Lorenzo V. Distribution and phylogeny of hexachlorocyclohexane-degrading bacteria in soils from Spain. Environ. Microbiol. 2006, 8:60-68.
    • (2006) Environ. Microbiol. , vol.8 , pp. 60-68
    • Mohn, W.W.1    Mertens, B.2    Neufeld, J.D.3    Verstraete, W.4    de Lorenzo, V.5
  • 8
    • 0033387054 scopus 로고    scopus 로고
    • Complete analysis of genes and enzymes for Γ-hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26
    • Nagata Y., Miyauchi K., Takagi M. Complete analysis of genes and enzymes for Γ-hexachlorocyclohexane degradation in Sphingomonas paucimobilis UT26. J. Ind. Microbiol. Biotechnol. 1999, 23:380-390.
    • (1999) J. Ind. Microbiol. Biotechnol. , vol.23 , pp. 380-390
    • Nagata, Y.1    Miyauchi, K.2    Takagi, M.3
  • 9
    • 13244265506 scopus 로고    scopus 로고
    • Identification and characterization of genes involved in the downstream degradation pathway of Γ-hexachlorocyclohexane in Sphingomonas paucimobilis UT26
    • Endo R., Kamakura M., Miyauchi K., Fukuda M., Ohtsubo Y., Tsuda M., Nagata Y. Identification and characterization of genes involved in the downstream degradation pathway of Γ-hexachlorocyclohexane in Sphingomonas paucimobilis UT26. J. Bacteriol. 2005, 187:847-853.
    • (2005) J. Bacteriol. , vol.187 , pp. 847-853
    • Endo, R.1    Kamakura, M.2    Miyauchi, K.3    Fukuda, M.4    Ohtsubo, Y.5    Tsuda, M.6    Nagata, Y.7
  • 10
    • 34548312340 scopus 로고    scopus 로고
    • Aerobic degradation of lindane (Γ-hexachlorocyclohexane) in bacteria and its biochemical and molecular basis
    • Nagata Y., Endo R., Ito M., Ohtsubo Y., Tsuda M. Aerobic degradation of lindane (Γ-hexachlorocyclohexane) in bacteria and its biochemical and molecular basis. Appl. Microbiol. Biotechnol. 2007, 76:741-752.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 741-752
    • Nagata, Y.1    Endo, R.2    Ito, M.3    Ohtsubo, Y.4    Tsuda, M.5
  • 11
    • 0025786069 scopus 로고
    • Molecular cloning of a Pseudomonas paucimobilis gene encoding a 17-kilodalton polypeptide that eliminates HCl molecules from Γ-hexachlorocyclohexane
    • Imai R., Nagata Y., Fukuda M., Takagi M., Yano K. Molecular cloning of a Pseudomonas paucimobilis gene encoding a 17-kilodalton polypeptide that eliminates HCl molecules from Γ-hexachlorocyclohexane. J. Bacteriol. 1991, 173:6811-6819.
    • (1991) J. Bacteriol. , vol.173 , pp. 6811-6819
    • Imai, R.1    Nagata, Y.2    Fukuda, M.3    Takagi, M.4    Yano, K.5
  • 12
    • 0027436421 scopus 로고
    • Cloning and sequencing of a dehalogenase gene encoding an enzyme with hydrolase activity involved in the degradation of Γ-hexachlorocyclohexane in Pseudomonas paucimobilis
    • Nagata Y., Nariya T., Ohtomo R., Fukuda M., Yano K., Takagi M. Cloning and sequencing of a dehalogenase gene encoding an enzyme with hydrolase activity involved in the degradation of Γ-hexachlorocyclohexane in Pseudomonas paucimobilis. J. Bacteriol. 1993, 175:6403-6410.
    • (1993) J. Bacteriol. , vol.175 , pp. 6403-6410
    • Nagata, Y.1    Nariya, T.2    Ohtomo, R.3    Fukuda, M.4    Yano, K.5    Takagi, M.6
  • 13
    • 84871380178 scopus 로고
    • Purification and characterization of Γ-hexachlorocyclohexane (Γ-HCH) dehydrochlorinase (LinA) from Pseudomonas paucimobilis
    • Nagata Y., Hatta T., Imai R., Kimbara K., Fukuda M., Yano K., Takagi M. Purification and characterization of Γ-hexachlorocyclohexane (Γ-HCH) dehydrochlorinase (LinA) from Pseudomonas paucimobilis. Biosci. Biotechnol. Biochem. 1993, 57:1582-1583.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1582-1583
    • Nagata, Y.1    Hatta, T.2    Imai, R.3    Kimbara, K.4    Fukuda, M.5    Yano, K.6    Takagi, M.7
  • 14
    • 0028276471 scopus 로고
    • Cloning and sequencing of a 2,5-dichloro-2,5-cyclohexadiene-1,4-diol dehydrogenase gene involved in the degradation of Γ-hexachlorocyclohexane in Pseudomonas paucimobilis
    • Nagata Y., Ohtomo R., Miyauchi K., Fukuda M., Yano K., Takagi M. Cloning and sequencing of a 2,5-dichloro-2,5-cyclohexadiene-1,4-diol dehydrogenase gene involved in the degradation of Γ-hexachlorocyclohexane in Pseudomonas paucimobilis. J. Bacteriol. 1994, 176:3117-3125.
    • (1994) J. Bacteriol. , vol.176 , pp. 3117-3125
    • Nagata, Y.1    Ohtomo, R.2    Miyauchi, K.3    Fukuda, M.4    Yano, K.5    Takagi, M.6
  • 15
    • 0031895255 scopus 로고    scopus 로고
    • Cloning and sequencing of a 2,5-dichlorohydroquinone reductive dehalogenase gene whose product is involved in degradation of gamma-hexachlorocyclohexane by Sphingomonas paucimobilis
    • Miyauchi K., Suh S.K., Nagata Y., Takagi M. Cloning and sequencing of a 2,5-dichlorohydroquinone reductive dehalogenase gene whose product is involved in degradation of gamma-hexachlorocyclohexane by Sphingomonas paucimobilis. J. Bacteriol. 1998, 180:1354-1359.
    • (1998) J. Bacteriol. , vol.180 , pp. 1354-1359
    • Miyauchi, K.1    Suh, S.K.2    Nagata, Y.3    Takagi, M.4
  • 16
    • 0032704711 scopus 로고    scopus 로고
    • Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose product is involved in degradation of Γ-hexachlorocyclohexane in Sphingomonas paucimobilis
    • Miyauchi K., Adachi Y., Nagata Y., Takagi M. Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose product is involved in degradation of Γ-hexachlorocyclohexane in Sphingomonas paucimobilis. J. Bacteriol. 1999, 181:6712-6719.
    • (1999) J. Bacteriol. , vol.181 , pp. 6712-6719
    • Miyauchi, K.1    Adachi, Y.2    Nagata, Y.3    Takagi, M.4
  • 19
    • 0017170103 scopus 로고
    • Metabolism of lindane in house flies: metabolic desaturation, dehydrogenation, and dehydrochlorination, and conjugation with glutathione
    • Tanaka K., Kurihara N., Nakajima M. Metabolism of lindane in house flies: metabolic desaturation, dehydrogenation, and dehydrochlorination, and conjugation with glutathione. Pestic. Biochem. Physiol. 1976, 6:392-399.
    • (1976) Pestic. Biochem. Physiol. , vol.6 , pp. 392-399
    • Tanaka, K.1    Kurihara, N.2    Nakajima, M.3
  • 20
    • 0035575802 scopus 로고    scopus 로고
    • Identification of protein fold and catalytic residues of Γ-hexachlorocyclohexane dehydrochlorinase LinA
    • Nagata Y., Mori K., Takagi M., Murzin A.G., Damborskỳ J. Identification of protein fold and catalytic residues of Γ-hexachlorocyclohexane dehydrochlorinase LinA. Proteins 2001, 45:471-477.
    • (2001) Proteins , vol.45 , pp. 471-477
    • Nagata, Y.1    Mori, K.2    Takagi, M.3    Murzin, A.G.4    Damborskỳ, J.5
  • 21
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 22
    • 0032558981 scopus 로고    scopus 로고
    • Structure-based design of potent inhibitors of scytalone dehydratase: displacement of a water molecule from the active site
    • Chen J.M., Xu S.L., Wawrzak Z., Basarab G.S., Jordan D.B. Structure-based design of potent inhibitors of scytalone dehydratase: displacement of a water molecule from the active site. Biochemistry 1998, 37:17735-17744.
    • (1998) Biochemistry , vol.37 , pp. 17735-17744
    • Chen, J.M.1    Xu, S.L.2    Wawrzak, Z.3    Basarab, G.S.4    Jordan, D.B.5
  • 23
    • 34047222146 scopus 로고    scopus 로고
    • Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1
    • Ferraro D.J., Brown E.N., Yu C.L., Parales R.E., Gibson D.T., Ramaswamy S. Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1. BMC Struct. Biol. 2007, 7:10.
    • (2007) BMC Struct. Biol. , vol.7 , pp. 10
    • Ferraro, D.J.1    Brown, E.N.2    Yu, C.L.3    Parales, R.E.4    Gibson, D.T.5    Ramaswamy, S.6
  • 24
    • 33845483902 scopus 로고    scopus 로고
    • The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1
    • Jakoncic J., Jouanneau Y., Meyer C., Stojanoff V. The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1. Biochem. Biophys. Res. Commun. 2007, 352:861-866.
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 861-866
    • Jakoncic, J.1    Jouanneau, Y.2    Meyer, C.3    Stojanoff, V.4
  • 25
    • 4444337310 scopus 로고    scopus 로고
    • Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1
    • Furusawa Y., Nagarajan V., Tanokura M., Masai E., Fukuda M., Senda T. Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1. J. Mol. Biol. 2004, 342:1041-1052.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1041-1052
    • Furusawa, Y.1    Nagarajan, V.2    Tanokura, M.3    Masai, E.4    Fukuda, M.5    Senda, T.6
  • 26
    • 18044377439 scopus 로고    scopus 로고
    • Structural insight into the dioxygenation of nitroarene compounds: the crystal structure of nitrobenzene dioxygenase
    • Friemann R., Ivkovic-Jensen M.M., Lessner D.J., Yu C.L., Gibson D.T., Parales R.E., et al. Structural insight into the dioxygenation of nitroarene compounds: the crystal structure of nitrobenzene dioxygenase. J. Mol. Biol. 2005, 348:1139-1151.
    • (2005) J. Mol. Biol. , vol.348 , pp. 1139-1151
    • Friemann, R.1    Ivkovic-Jensen, M.M.2    Lessner, D.J.3    Yu, C.L.4    Gibson, D.T.5    Parales, R.E.6
  • 27
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 1993, 233:123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 28
    • 0030593377 scopus 로고    scopus 로고
    • The 1.6Å resolution crystal structure of nuclear transport factor 2 (NTF2)
    • Bullock T.L., Clarkson W.D., Kent H.M., Stewart M. The 1.6Å resolution crystal structure of nuclear transport factor 2 (NTF2). J. Mol. Biol. 1996, 260:422-431.
    • (1996) J. Mol. Biol. , vol.260 , pp. 422-431
    • Bullock, T.L.1    Clarkson, W.D.2    Kent, H.M.3    Stewart, M.4
  • 31
    • 33644766092 scopus 로고    scopus 로고
    • Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity
    • Kallio P., Sultana A., Niemi J., Mäntsälä P., Schneider G. Crystal structure of the polyketide cyclase AknH with bound substrate and product analogue: implications for catalytic mechanism and product stereoselectivity. J. Mol. Biol. 2006, 357:210-220.
    • (2006) J. Mol. Biol. , vol.357 , pp. 210-220
    • Kallio, P.1    Sultana, A.2    Niemi, J.3    Mäntsälä, P.4    Schneider, G.5
  • 32
    • 0042065062 scopus 로고    scopus 로고
    • Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15
    • Fribourg S., Conti E. Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15. EMBO Rep. 2003, 4:699-703.
    • (2003) EMBO Rep. , vol.4 , pp. 699-703
    • Fribourg, S.1    Conti, E.2
  • 33
    • 3142559476 scopus 로고    scopus 로고
    • Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation
    • Sultana A., Kallio P., Jansson A., Wang J.S., Niemi J., Mäntsälä P., Schneider G. Structure of the polyketide cyclase SnoaL reveals a novel mechanism for enzymatic aldol condensation. EMBO J. 2004, 23:1911-1921.
    • (2004) EMBO J. , vol.23 , pp. 1911-1921
    • Sultana, A.1    Kallio, P.2    Jansson, A.3    Wang, J.S.4    Niemi, J.5    Mäntsälä, P.6    Schneider, G.7
  • 34
    • 0037863737 scopus 로고    scopus 로고
    • Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
    • Arand M., Hallberg B.M., Zou J., Bergfors T., Oesch F., van der Werf M.J., et al. Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site. EMBO J. 2003, 22:2583-2592.
    • (2003) EMBO J. , vol.22 , pp. 2583-2592
    • Arand, M.1    Hallberg, B.M.2    Zou, J.3    Bergfors, T.4    Oesch, F.5    van der Werf, M.J.6
  • 35
    • 0032013251 scopus 로고    scopus 로고
    • CDNA cloning, expression, and mutagenesis of scytalone dehydratase needed for pathogenicity of the rice blast fungus, Pyricularia oryzae
    • Motoyama T., Imanishi K., Yamaguchi I. cDNA cloning, expression, and mutagenesis of scytalone dehydratase needed for pathogenicity of the rice blast fungus, Pyricularia oryzae. Biosci. Biotechnol. Biochem. 1998, 62:564-566.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 564-566
    • Motoyama, T.1    Imanishi, K.2    Yamaguchi, I.3
  • 36
    • 0002392821 scopus 로고    scopus 로고
    • Inhibition of scytalone dehydratase in melanin biosynthesis by carpropamid, a novel rice blast controlling agent
    • Motoyama T., Imanishi K., Kinbara T., Kurahashi Y., Yamaguchi I. Inhibition of scytalone dehydratase in melanin biosynthesis by carpropamid, a novel rice blast controlling agent. J. Pestic. Sci. 1998, 23:58-61.
    • (1998) J. Pestic. Sci. , vol.23 , pp. 58-61
    • Motoyama, T.1    Imanishi, K.2    Kinbara, T.3    Kurahashi, Y.4    Yamaguchi, I.5
  • 37
    • 68649105232 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of γ-hexachlorocyclohexane dehydrochlorinase LinA from Sphingobium japonicum UT26
    • Okai M., Kubota K., Fukuda M., Nagata Y., Nagata K., Tanokura M. Crystallization and preliminary X-ray analysis of γ-hexachlorocyclohexane dehydrochlorinase LinA from Sphingobium japonicum UT26. Acta Crystallogr. Sect. F 2009, 65:822-824.
    • (2009) Acta Crystallogr. Sect. F , vol.65 , pp. 822-824
    • Okai, M.1    Kubota, K.2    Fukuda, M.3    Nagata, Y.4    Nagata, K.5    Tanokura, M.6
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 1999, 6:458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 41
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 1999, 125:156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 42
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A.A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.A.1    Teplyakov, A.2
  • 44
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 1997, 53:240-255.
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3


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