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Volumn 287, Issue 31, 2012, Pages 26213-26222

The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain

Author keywords

[No Author keywords available]

Indexed keywords

ACINETOBACTERS; AUTOINHIBITORY DOMAIN; BACTERIAL ANTIBIOTIC RESISTANCE; BAUMANNII; C-TERMINAL DOMAINS; CATALYTIC PROPERTIES; CONFORMATIONAL CHANGE; FLAVIN REDUCTASE; N-TERMINAL DOMAINS; OXYGENASES; RATE OF REDUCTION; SINGLE SITES; SINGLE-SITE MUTATIONS; WILD-TYPE ENZYMES;

EID: 84864381297     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.354472     Document Type: Article
Times cited : (23)

References (48)
  • 1
    • 69249142914 scopus 로고    scopus 로고
    • Regulation of interdomain electron transfer in the NOS output state for NO production
    • Feng, C., and Tollin, G. (2009) Regulation of interdomain electron transfer in the NOS output state for NO production. Dalton Trans. 34, 6692-6700
    • (2009) Dalton Trans. , vol.34 , pp. 6692-6700
    • Feng, C.1    Tollin, G.2
  • 2
    • 78649450474 scopus 로고    scopus 로고
    • Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450
    • Laursen, T., Jensen, K., and Møller, B. L. (2011) Conformational changes of the NADPH-dependent cytochrome P450 reductase in the course of electron transfer to cytochromes P450. Biochim. Biophys. Acta 1814, 132-138
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 132-138
    • Laursen, T.1    Jensen, K.2    Møller, B.L.3
  • 3
    • 71049135329 scopus 로고    scopus 로고
    • Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase
    • Xia, C., Misra, I., Iyanagi, T., and Kim, J. J. (2009) Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase. J. Biol. Chem. 284, 30708-30717
    • (2009) J. Biol. Chem. , vol.284 , pp. 30708-30717
    • Xia, C.1    Misra, I.2    Iyanagi, T.3    Kim, J.J.4
  • 4
    • 79955543878 scopus 로고    scopus 로고
    • Conformational changes of NADPH-cytochrome P450 oxidoreductase are essential for catalysis and cofactor binding
    • Xia, C., Hamdane, D., Shen, A. L., Choi, V., Kasper, C. B., Pearl, N. M., Zhang, H., Im, S. C., Waskell, L., and Kim, J. J. (2011) Conformational changes of NADPH-cytochrome P450 oxidoreductase are essential for catalysis and cofactor binding. J. Biol. Chem. 286, 16246-16260
    • (2011) J. Biol. Chem. , vol.286 , pp. 16246-16260
    • Xia, C.1    Hamdane, D.2    Shen, A.L.3    Choi, V.4    Kasper, C.B.5    Pearl, N.M.6    Zhang, H.7    Im, S.C.8    Waskell, L.9    Kim, J.J.10
  • 5
    • 73649109571 scopus 로고    scopus 로고
    • Domain motion in cytochrome P450 reductase: Conformational equilibria revealed by NMR and small-angle x-ray scattering
    • Ellis, J., Gutierrez, A., Barsukov, I. L., Huang, W. C., Grossmann, J. G., and Roberts, G. C. (2009) Domain motion in cytochrome P450 reductase: conformational equilibria revealed by NMR and small-angle x-ray scattering. J. Biol. Chem. 284, 36628-36637
    • (2009) J. Biol. Chem. , vol.284 , pp. 36628-36637
    • Ellis, J.1    Gutierrez, A.2    Barsukov, I.L.3    Huang, W.C.4    Grossmann, J.G.5    Roberts, G.C.6
  • 6
    • 77449150569 scopus 로고    scopus 로고
    • Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transfer
    • Guan, Z. W., Haque, M. M., Wei, C. C., Garcin, E. D., Getzoff, E. D., and Stuehr, D. J. (2010) Lys842 in neuronal nitric-oxide synthase enables the autoinhibitory insert to antagonize calmodulin binding, increase FMN shielding, and suppress interflavin electron transfer. J. Biol. Chem. 285, 3064-3075
    • (2010) J. Biol. Chem. , vol.285 , pp. 3064-3075
    • Guan, Z.W.1    Haque, M.M.2    Wei, C.C.3    Garcin, E.D.4    Getzoff, E.D.5    Stuehr, D.J.6
  • 7
    • 0034703091 scopus 로고    scopus 로고
    • The C termini of constitutive nitric-oxide synthases control electron flow through the flavin and heme domains and affect modulation by calmodulin
    • DOI 10.1074/jbc.M004766200
    • Roman, L. J., Martásek, P., Miller, R. T., Harris, D. E., de La Garza, M. A., Shea, T. M., Kim, J. J., and Masters, B. S. (2000) The C termini of constitutive nitric-oxide synthases control electron flow through the flavin and heme domains and affect modulation by calmodulin. J. Biol. Chem. 275, 29225-29232 (Pubitemid 32043790)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29225-29232
    • Roman, L.J.1    Martasek, P.2    Miller, R.T.3    Harris, D.E.4    De La, G.M.A.5    Shea, T.M.6    Kim, J.-J.P.7    Masters, B.S.S.8
  • 8
    • 39049118381 scopus 로고    scopus 로고
    • Activity coupling and complex formation between bacterial luciferase and flavin reductases
    • Tu, S. C. (2008) Activity coupling and complex formation between bacterial luciferase and flavin reductases. Photochem. Photobiol. Sci. 7, 183-188
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 183-188
    • Tu, S.C.1
  • 9
    • 0038206661 scopus 로고    scopus 로고
    • Energy transfer evidence for in vitro and in vivo complexes of Vibrio harveyi flavin reductase P and luciferase
    • Low, J. C., and Tu, S. C. (2003) Energy transfer evidence for in vitro and in vivo complexes of Vibrio harveyi flavin reductase P and luciferase. Photochem. Photobiol. 77, 446-452
    • (2003) Photochem. Photobiol. , vol.77 , pp. 446-452
    • Low, J.C.1    Tu, S.C.2
  • 10
    • 77952545697 scopus 로고    scopus 로고
    • The FMN-dependent two-component monooxygenase systems
    • Ellis, H. R. (2010) The FMN-dependent two-component monooxygenase systems. Arch. Biochem. Biophys. 497, 1-12
    • (2010) Arch. Biochem. Biophys. , vol.497 , pp. 1-12
    • Ellis, H.R.1
  • 11
    • 33751560654 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli
    • DOI 10.1128/JB.00966-06
    • Abdurachim, K., and Ellis, H. R. (2006) Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli. J. Bacteriol. 188, 8153-8159 (Pubitemid 44845686)
    • (2006) Journal of Bacteriology , vol.188 , Issue.23 , pp. 8153-8159
    • Abdurachim, K.1    Ellis, H.R.2
  • 12
    • 34547095238 scopus 로고    scopus 로고
    • Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase
    • DOI 10.1021/bi7006614
    • Sucharitakul, J., Phongsak, T., Entsch, B., Svasti, J., Chaiyen, P., and Ballou, D. P. (2007) Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase. Biochemistry 46, 8611-8623 (Pubitemid 47106112)
    • (2007) Biochemistry , vol.46 , Issue.29 , pp. 8611-8623
    • Sucharitakul, J.1    Phongsak, T.2    Entsch, B.3    Svasti, J.4    Chaiyen, P.5    Ballou, D.P.6
  • 13
    • 44849143455 scopus 로고    scopus 로고
    • Mechanism and regulation of the two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor
    • Valton, J., Mathevon, C., Fontecave, M., Nivière, V., and Ballou, D. P. (2008) Mechanism and regulation of the two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor. J. Biol. Chem. 283, 10287-10296
    • (2008) J. Biol. Chem. , vol.283 , pp. 10287-10296
    • Valton, J.1    Mathevon, C.2    Fontecave, M.3    Nivière, V.4    Ballou, D.P.5
  • 14
    • 24944534515 scopus 로고    scopus 로고
    • Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase
    • DOI 10.1016/j.abb.2005.07.020, PII S0003986105003061
    • Kantz, A., Chin, F., Nallamothu, N., Nguyen, T., and Gassner, G. T. (2005) Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase. Arch. Biochem. Biophys. 442, 102-116 (Pubitemid 41330996)
    • (2005) Archives of Biochemistry and Biophysics , vol.442 , Issue.1 , pp. 102-116
    • Kantz, A.1    Chin, F.2    Nallamothu, N.3    Nguyen, T.4    Gassner, G.T.5
  • 15
    • 75349094072 scopus 로고    scopus 로고
    • Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: A system composed of a small flavin reductase and a large flavin-dependent oxygenase
    • Chakraborty, S., Ortiz-Maldonado, M., Entsch, B., and Ballou, D. P. (2010) Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase. Biochemistry 49, 372-385
    • (2010) Biochemistry , vol.49 , pp. 372-385
    • Chakraborty, S.1    Ortiz-Maldonado, M.2    Entsch, B.3    Ballou, D.P.4
  • 16
    • 0028049081 scopus 로고
    • Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme
    • Arunachalam, U., Massey, V., and Miller, S. M. (1994) Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme. J. Biol. Chem. 269, 150-155 (Pubitemid 24026637)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.1 , pp. 150-155
    • Arunachalam, U.1    Massey, V.2    Miller, S.M.3
  • 17
    • 0028277937 scopus 로고
    • Studies on the oxidative half-reaction of p-hydroxyphenylacetate 3-hydroxylase
    • Arunachalam, U., and Massey, V. (1994) Studies on the oxidative half-reaction of p-hydroxyphenylacetate 3-hydroxylase. J. Biol. Chem. 269, 11795-11801
    • (1994) J. Biol. Chem. , vol.269 , pp. 11795-11801
    • Arunachalam, U.1    Massey, V.2
  • 18
    • 0342514774 scopus 로고    scopus 로고
    • Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: A prototype of a new flavin:NAD(P)H reductase subfamily
    • Galán, B., Díaz, E., Prieto, M. A., and García, J. L. (2000) Functional analysis of the small component of the 4- hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: a prototype of a new flavin:NAD(P)H reductase subfamily. J. Bacteriol. 182, 627-636
    • (2000) J. Bacteriol. , vol.182 , pp. 627-636
    • Galán, B.1    Díaz, E.2    Prieto, M.A.3    García, J.L.4
  • 19
    • 0030898946 scopus 로고    scopus 로고
    • Molecular cloning and analysis of the genes encoding the 4-hydroxyphenylacetate hydroxylase from Klebsiella pneumoniae
    • Gibello, A., Suárez, M., Allende, J. L., and Martin, M. (1997) Molecular cloning and analysis of the genes encoding the 4-hydroxyphenylacetate hydroxylase from Klebsiella pneumoniae. Arch. Microbiol. 167, 160 -166
    • (1997) Arch. Microbiol. , vol.167 , pp. 160-166
    • Gibello, A.1    Suárez, M.2    Allende, J.L.3    Martin, M.4
  • 21
    • 36348950818 scopus 로고    scopus 로고
    • Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8
    • DOI 10.1074/jbc.M703440200
    • Kim, S. H., Hisano, T., Takeda, K., Iwasaki, W., Ebihara, A., and Miki, K. (2007) Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8. J. Biol. Chem. 282, 33107-33117 (Pubitemid 350159282)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.45 , pp. 33107-33117
    • Kim, S.-H.1    Hisano, T.2    Takeda, K.3    Iwasaki, W.4    Ebihara, A.5    Miki, K.6
  • 22
    • 38549124488 scopus 로고    scopus 로고
    • Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity
    • DOI 10.1002/prot.21534
    • Kim, S. H., Hisano, T., Iwasaki, W., Ebihara, A., and Miki, K. (2008) Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: structural basis for the flavin affinity. Proteins 70, 718-730 (Pubitemid 351161933)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.3 , pp. 718-730
    • Kim, S.-H.1    Hisano, T.2    Iwasaki, W.3    Ebihara, A.4    Miki, K.5
  • 23
    • 0035722573 scopus 로고    scopus 로고
    • A novel two-protein component flavoprotein hydroxylase
    • Chaiyen, P., Suadee, C., and Wilairat, P. (2001) A novel two-protein component flavoprotein hydroxylase. Eur. J. Biochem. 268, 5550-5561
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5550-5561
    • Chaiyen, P.1    Suadee, C.2    Wilairat, P.3
  • 24
    • 4644255461 scopus 로고    scopus 로고
    • Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: Evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases
    • DOI 10.1016/j.bbaexp.2004.08.003, PII S0167478104001502
    • Thotsaporn, K., Sucharitakul, J., Wongratana, J., Suadee, C., and Chaiyen, P. (2004) Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases. Biochim. Biophys. Acta 1680, 60-66 (Pubitemid 39286743)
    • (2004) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1680 , Issue.1 , pp. 60-66
    • Thotsaporn, K.1    Sucharitakul, J.2    Wongratana, J.3    Suadee, C.4    Chaiyen, P.5
  • 25
    • 23044506644 scopus 로고    scopus 로고
    • The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis
    • DOI 10.1021/bi050615e
    • Sucharitakul, J., Chaiyen, P., Entsch, B., and Ballou, D. P. (2005) The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis. Biochemistry 44, 10434-10442 (Pubitemid 41076839)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10434-10442
    • Sucharitakul, J.1    Chaiyen, P.2    Entsch, B.3    Ballou, D.P.4
  • 26
    • 33745211234 scopus 로고    scopus 로고
    • Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii
    • Sucharitakul, J., Chaiyen, P., Entsch, B., and Ballou, D. P. (2006) Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii. J. Biol. Chem. 281, 17044-17053
    • (2006) J. Biol. Chem. , vol.281 , pp. 17044-17053
    • Sucharitakul, J.1    Chaiyen, P.2    Entsch, B.3    Ballou, D.P.4
  • 28
    • 67649214510 scopus 로고    scopus 로고
    • Ultrafast solvation dynamics of flavin mononucleotide in the reductase component of p-hydroxyphenylacetate hydroxylase
    • Chosrowjan, H., Taniguchi, S., Mataga, N., Phongsak, T., Sucharitakul, J., Chaiyen, P., and Tanaka, F. (2009) Ultrafast solvation dynamics of flavin mononucleotide in the reductase component of p-hydroxyphenylacetate hydroxylase. J. Phys. Chem. B 113, 8439-8442
    • (2009) J. Phys. Chem. B , vol.113 , pp. 8439-8442
    • Chosrowjan, H.1    Taniguchi, S.2    Mataga, N.3    Phongsak, T.4    Sucharitakul, J.5    Chaiyen, P.6    Tanaka, F.7
  • 29
    • 78650947225 scopus 로고    scopus 로고
    • pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase
    • Ruangchan, N., Tongsook, C., Sucharitakul, J., and Chaiyen, P. (2011) pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase. J. Biol. Chem. 286, 223-233
    • (2011) J. Biol. Chem. , vol.286 , pp. 223-233
    • Ruangchan, N.1    Tongsook, C.2    Sucharitakul, J.3    Chaiyen, P.4
  • 30
    • 80051480273 scopus 로고    scopus 로고
    • Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms
    • Thotsaporn, K., Chenprakhon, P., Sucharitakul, J., Mattevi, A., and Chaiyen, P. (2011) Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms. J. Biol. Chem. 286, 28170-28180
    • (2011) J. Biol. Chem. , vol.286 , pp. 28170-28180
    • Thotsaporn, K.1    Chenprakhon, P.2    Sucharitakul, J.3    Mattevi, A.4    Chaiyen, P.5
  • 31
    • 84455161802 scopus 로고    scopus 로고
    • Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase
    • Tongsook, C., Sucharitakul, J., Thotsaporn, K., and Chaiyen, P. (2011) Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase. J. Biol. Chem. 286, 44491-44502
    • (2011) J. Biol. Chem. , vol.286 , pp. 44491-44502
    • Tongsook, C.1    Sucharitakul, J.2    Thotsaporn, K.3    Chaiyen, P.4
  • 32
    • 0026532662 scopus 로고
    • Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter " strain ATCC 29600
    • Uetz, T., Schneider, R., Snozzi, M., and Egli, T. (1992) Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter " strain ATCC 29600. J. Bacteriol. 174, 1179-1188
    • (1992) J. Bacteriol. , vol.174 , pp. 1179-1188
    • Uetz, T.1    Schneider, R.2    Snozzi, M.3    Egli, T.4
  • 33
    • 0030728465 scopus 로고    scopus 로고
    • Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103
    • Witschel, M., Nagel, S., and Egli, T. (1997) Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103. J. Bacteriol. 179, 6937-6943 (Pubitemid 27492475)
    • (1997) Journal of Bacteriology , vol.179 , Issue.22 , pp. 6937-6943
    • Witschel, M.1    Nagel, S.2    Egli, T.3
  • 34
    • 33745991798 scopus 로고    scopus 로고
    • Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
    • DOI 10.1016/j.jbiotec.2006.03.044, PII S016816560600318X
    • 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 (Pubitemid 44066596)
    • (2006) Journal of Biotechnology , vol.124 , Issue.4 , pp. 670-689
    • Van Berkel, W.J.H.1    Kamerbeek, N.M.2    Fraaije, M.W.3
  • 35
    • 1842424838 scopus 로고    scopus 로고
    • Structural Studies on Flavin Reductase PheA2 Reveal Binding of NAD in an Unusual Folded Conformation and Support Novel Mechanism of Action
    • DOI 10.1074/jbc.M313765200
    • van den Heuvel, R. H., Westphal, A. H., Heck, A. J., Walsh, M. A., Rovida, S., van Berkel, W. J., and Mattevi, A. (2004) Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action. J. Biol. Chem. 279, 12860-12867 (Pubitemid 38445860)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12860-12867
    • Van Den, H.R.H.H.1    Westphal, A.H.2    Heck, A.J.R.3    Walsh, M.A.4    Rovida, S.5    Van Berkel, W.J.H.6    Mattevi, A.7
  • 36
    • 40649118187 scopus 로고    scopus 로고
    • Structural insight on the mechanism of regulation of the MarR family of proteins: High-resolution crystal structure of a transcriptional repressor from Methanobacterium thermoautotrophicum
    • Saridakis, V., Shahinas, D., Xu, X., and Christendat, D. (2008) Structural insight on the mechanism of regulation of the MarR family of proteins: high-resolution crystal structure of a transcriptional repressor from Methanobacterium thermoautotrophicum. J. Mol. Biol. 377, 655-667
    • (2008) J. Mol. Biol. , vol.377 , pp. 655-667
    • Saridakis, V.1    Shahinas, D.2    Xu, X.3    Christendat, D.4
  • 37
    • 0032844440 scopus 로고    scopus 로고
    • The mar regulon: Multiple resistance to antibiotics and other toxic chemicals
    • DOI 10.1016/S0966-842X(99)01589-9, PII S0966842X99015899
    • Alekshun, M. N., and Levy, S. B. (1999) The mar regulon: multiple resistance to antibiotics and other toxic chemicals. Trends Microbiol. 7, 410-413 (Pubitemid 29450465)
    • (1999) Trends in Microbiology , vol.7 , Issue.10 , pp. 410-413
    • Alekshun, M.N.1    Levy, S.B.2
  • 38
    • 0034887133 scopus 로고    scopus 로고
    • The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution
    • DOI 10.1038/90429
    • Alekshun, M. N., Levy, S. B., Mealy, T. R., Seaton, B. A., and Head, J. F. (2001) The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution. Nat. Struct. Biol. 8, 710-714 (Pubitemid 32757932)
    • (2001) Nature Structural Biology , vol.8 , Issue.8 , pp. 710-714
    • Alekshun, M.N.1    Levy, S.B.2    Mealy, T.R.3    Seaton, B.A.4    Head, J.F.5
  • 39
    • 0015156378 scopus 로고
    • A sensitive method for the determination of RNA in DNA and vice versa
    • Duch, D. S., and Laskowski, M., Sr. (1971) A sensitive method for the determination of RNA in DNA and vice versa. Anal. Biochem. 44, 42-48
    • (1971) Anal. Biochem. , vol.44 , pp. 42-48
    • Duch, D.S.1    Laskowski Sr., M.2
  • 40
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723 (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 41
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385 (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 42
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201 (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 44
    • 84862164693 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii
    • Oonanant, W., Sucharitakul, J., Chaiyen, P., and Yuvaniyama, J. (2012) Crystallization and preliminary x-ray analysis of the reductase component of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68, 720-723
    • (2012) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.68 , pp. 720-723
    • Oonanant, W.1    Sucharitakul, J.2    Chaiyen, P.3    Yuvaniyama, J.4
  • 46
    • 0034681382 scopus 로고    scopus 로고
    • Removal of a putative inhibitory element reduces the calcium-dependent calmodulin activation of neuronal nitric-oxide synthase
    • Montgomery, H. J., Romanov, V., and Guillemette, J. G. (2000) Removal of a putative inhibitory element reduces the calcium-dependent calmodulin activation of neuronal nitric-oxide synthase. J. Biol. Chem. 275, 5052-5058
    • (2000) J. Biol. Chem. , vol.275 , pp. 5052-5058
    • Montgomery, H.J.1    Romanov, V.2    Guillemette, J.G.3
  • 47
    • 0008632745 scopus 로고    scopus 로고
    • Autoinhibition of endothelial nitric-oxide synthase. Identification of an electron transfer control element
    • Nishida, C. R., and Ortiz de Montellano P. R. (1999) Autoinhibition of endothelial nitric-oxide synthase. Identification of an electron transfer control element. J. Biol. Chem. 274, 14692-14698
    • (1999) J. Biol. Chem. , vol.274 , pp. 14692-14698
    • Nishida, C.R.1    Ortiz De Montellano, P.R.2
  • 48
    • 51849113324 scopus 로고    scopus 로고
    • Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain
    • Welland, A., Garnaud, P. E., Kitamura, M., Miles, C. S., and Daff, S. (2008) Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain. Biochemistry 47, 9771-9780
    • (2008) Biochemistry , vol.47 , pp. 9771-9780
    • Welland, A.1    Garnaud, P.E.2    Kitamura, M.3    Miles, C.S.4    Daff, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.