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Volumn 348, Issue 2, 2005, Pages 363-382

Crystal structure of the mosquito-larvicidal toxin Cry4Ba and its biological implications

Author keywords

Bioinsecticide; Hydrophobic patch; Proteolytic activation; Target specificity; Toxin membrane interaction

Indexed keywords

CRY4BA TOXIN; LARVICIDAL AGENT; TOXIN; UNCLASSIFIED DRUG;

EID: 16244392435     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.02.013     Document Type: Article
Times cited : (207)

References (80)
  • 1
    • 0028002221 scopus 로고
    • Mechanism of action of Bacillus thuringiensis insecticidal delta-endotoxins
    • B.H. Knowles Mechanism of action of Bacillus thuringiensis insecticidal delta-endotoxins Advan. Insect Physiol. 24 1994 275 308
    • (1994) Advan. Insect Physiol. , vol.24 , pp. 275-308
    • Knowles, B.H.1
  • 3
    • 0028291484 scopus 로고
    • The receptor of Bacillus thuringiensis CryIA(c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N
    • P.J.K. Knight, N. Crickmore, and D.J. Ellar The receptor of Bacillus thuringiensis CryIA(c) delta-endotoxin in the brush border membrane of the lepidopteran Manduca sexta is aminopeptidase N Mol. Microbiol. 11 1994 429 436
    • (1994) Mol. Microbiol. , vol.11 , pp. 429-436
    • Knight, P.J.K.1    Crickmore, N.2    Ellar, D.J.3
  • 4
    • 0029027032 scopus 로고
    • Molecular cloning of an insect aminopeptidase N that serves as a receptor for Bacillus thuringiensis CryIA(c) toxin
    • P.J.K. Knight, B.H. Knowles, and D.J. Ellar Molecular cloning of an insect aminopeptidase N that serves as a receptor for Bacillus thuringiensis CryIA(c) toxin J. Biol. Chem. 270 1995 17765 17770
    • (1995) J. Biol. Chem. , vol.270 , pp. 17765-17770
    • Knight, P.J.K.1    Knowles, B.H.2    Ellar, D.J.3
  • 6
    • 0027258633 scopus 로고
    • Specific binding protein from Manduca sexta for the insecticidal toxin of Bacillus thuringiensis subsp. berliner
    • R.K. Vadlamudi, T.H. Ji, and L.A. Bulla Jr specific binding protein from Manduca sexta for the insecticidal toxin of Bacillus thuringiensis subsp. berliner J. Biol. Chem. 268 1993 12334 12340
    • (1993) J. Biol. Chem. , vol.268 , pp. 12334-12340
    • Vadlamudi, R.K.1    Ji, T.H.2    Bulla Jr., L.A.3
  • 7
    • 0028907322 scopus 로고
    • Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis
    • R.K. Vadlamudi, E. Weber, I. Ji, T.H. Ji, and L.A. Bulla Jr Cloning and expression of a receptor for an insecticidal toxin of Bacillus thuringiensis J. Biol. Chem. 270 1995 5490 5494
    • (1995) J. Biol. Chem. , vol.270 , pp. 5490-5494
    • Vadlamudi, R.K.1    Weber, E.2    Ji, I.3    Ji, T.H.4    Bulla Jr., L.A.5
  • 8
    • 0022559319 scopus 로고
    • Characterisation and partial purification of a plasma membrane receptor from Bacillus thuringiensis var. kurstaki lepidopteran-specific δ-endotoxins
    • B.H. Knowles, and D.J. Ellar Characterisation and partial purification of a plasma membrane receptor from Bacillus thuringiensis var. kurstaki lepidopteran-specific δ-endotoxins J. Cell Sci. 83 1986 89 101
    • (1986) J. Cell Sci. , vol.83 , pp. 89-101
    • Knowles, B.H.1    Ellar, D.J.2
  • 9
    • 0025871617 scopus 로고
    • N-acetyl galactosamine is part of the receptor in insect gut epithelia that recognizes an insecticidal protein from Bacillus thuringiensis
    • B.H. Knowles, P.J.K. Knight, and D.J. Ellar N-acetyl galactosamine is part of the receptor in insect gut epithelia that recognizes an insecticidal protein from Bacillus thuringiensis Proc. Roy. Soc. ser. B 245 1991 31 35
    • (1991) Proc. Roy. Soc. Ser. B , vol.245 , pp. 31-35
    • Knowles, B.H.1    Knight, P.J.K.2    Ellar, D.J.3
  • 10
    • 0032142903 scopus 로고    scopus 로고
    • Bacillus thuringiensis Cry1Ac toxin interaction with Manduca sexta aminopeptidase N in a model membrane environment
    • M.A. Cooper, J. Carroll, E.R. Travis, D.H. Williams, and D.J. Ellar Bacillus thuringiensis Cry1Ac toxin interaction with Manduca sexta aminopeptidase N in a model membrane environment Biochem. J. 333 1998 677 683
    • (1998) Biochem. J. , vol.333 , pp. 677-683
    • Cooper, M.A.1    Carroll, J.2    Travis, E.R.3    Williams, D.H.4    Ellar, D.J.5
  • 11
    • 0023183759 scopus 로고
    • Colloid-osmotic lysis is a general feature of the mechanism of action of Bacillus thuringiensis δ-endotoxins with different specificity
    • B.H. Knowles, and D.J. Ellar Colloid-osmotic lysis is a general feature of the mechanism of action of Bacillus thuringiensis δ-endotoxins with different specificity Biochim. Biophys. Acta 924 1987 509 518
    • (1987) Biochim. Biophys. Acta , vol.924 , pp. 509-518
    • Knowles, B.H.1    Ellar, D.J.2
  • 12
    • 0026050639 scopus 로고
    • Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution
    • J. Li, J. Carroll, and D.J. Ellar Crystal structure of insecticidal δ-endotoxin from Bacillus thuringiensis at 2.5 Å resolution Nature 353 1991 815 821
    • (1991) Nature , vol.353 , pp. 815-821
    • Li, J.1    Carroll, J.2    Ellar, D.J.3
  • 15
    • 0035214724 scopus 로고    scopus 로고
    • Crystallization of the Bacillus thuringiensis toxin Cry1Ac and its complex with the receptor ligand N-acetyl-D-galactosamine
    • D.J. Derbyshire, D.J. Ellar, and J. Li Crystallization of the Bacillus thuringiensis toxin Cry1Ac and its complex with the receptor ligand N-acetyl-D-galactosamine Acta Crystallog. sect. D 57 2001 1938 1944
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 1938-1944
    • Derbyshire, D.J.1    Ellar, D.J.2    Li, J.3
  • 16
    • 0034859678 scopus 로고    scopus 로고
    • Structural implications for the transformation of the Bacillus thuringiensis δ-endotoxins from water-soluble to membrane-inserted forms
    • J. Li, D.J. Derbyshire, B. Promdonkoy, and D.J. Ellar Structural implications for the transformation of the Bacillus thuringiensis δ-endotoxins from water-soluble to membrane-inserted forms Biochem. Soc. Trans. 29 2001 571 577
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 571-577
    • Li, J.1    Derbyshire, D.J.2    Promdonkoy, B.3    Ellar, D.J.4
  • 17
    • 0034980642 scopus 로고    scopus 로고
    • Structure of Cry2Aa suggests an unexpected receptor binding epitope
    • R.J. Morse, T. Yamamoto, and R.M. Stroud Structure of Cry2Aa suggests an unexpected receptor binding epitope Structure 9 2001 409 417
    • (2001) Structure , vol.9 , pp. 409-417
    • Morse, R.J.1    Yamamoto, T.2    Stroud, R.M.3
  • 18
    • 0025138436 scopus 로고
    • Directed mutagenesis of selected regions of a Bacillus thuringiensis entomocidal protein
    • W. Ahmad, and D.J. Ellar Directed mutagenesis of selected regions of a Bacillus thuringiensis entomocidal protein FEMS Microbiol. Letters 68 1990 97 104
    • (1990) FEMS Microbiol. Letters , vol.68 , pp. 97-104
    • Ahmad, W.1    Ellar, D.J.2
  • 19
    • 0026785278 scopus 로고
    • Localised mutagenesis defines regions of the Bacillus thuringiensis δ-endotoxin involved in toxicity and specificity
    • D. Wu, and A.I. Aronson Localised mutagenesis defines regions of the Bacillus thuringiensis δ-endotoxin involved in toxicity and specificity J. Biol. Chem. 267 1992 2311 2317
    • (1992) J. Biol. Chem. , vol.267 , pp. 2311-2317
    • Wu, D.1    Aronson, A.I.2
  • 20
    • 0030785699 scopus 로고    scopus 로고
    • Restriction of intramolecular movements within the Cry1Aa toxin molecule of Bacillus thuringiensis through disulfide bond engineering
    • J.-L. Schwartz, M. Juteau, P. Grochulski, M. Cygler, G. Prefontaine, R. Brousseau, and L. Masson Restriction of intramolecular movements within the Cry1Aa toxin molecule of Bacillus thuringiensis through disulfide bond engineering FEBS Letters 410 1997 397 402
    • (1997) FEBS Letters , vol.410 , pp. 397-402
    • Schwartz, J.-L.1    Juteau, M.2    Grochulski, P.3    Cygler, M.4    Prefontaine, G.5    Brousseau, R.6    Masson, L.7
  • 21
    • 0024687823 scopus 로고
    • Location of the Bombyx mori specificity domain on a Bacillus thuringiensis δ-endotoxin protein
    • A.Z. Ge, N.I. Shivarova, and D.H. Dean Location of the Bombyx mori specificity domain on a Bacillus thuringiensis δ-endotoxin protein Proc. Natl Acad. Sci. USA 86 1989 4037 4041
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4037-4041
    • Ge, A.Z.1    Shivarova, N.I.2    Dean, D.H.3
  • 22
    • 0025670009 scopus 로고
    • Specificity determining regions of a lepidopteran-specific insecticidal protein produced by Bacillus thuringiensis
    • H.E. Schnepf, K. Tomezak, J.P. Ortega, and H.R. Whiteley Specificity determining regions of a lepidopteran-specific insecticidal protein produced by Bacillus thuringiensis J. Biol. Chem. 265 1990 20923 20930
    • (1990) J. Biol. Chem. , vol.265 , pp. 20923-20930
    • Schnepf, H.E.1    Tomezak, K.2    Ortega, J.P.3    Whiteley, H.R.4
  • 23
    • 0027997324 scopus 로고
    • Mutagenesis of two surface-exposed loops of a Bacillus thuringiensis CryIC δ-endotoxin affects insecticidal specificity
    • G.P. Smith, and D.J. Ellar Mutagenesis of two surface-exposed loops of a Bacillus thuringiensis CryIC δ-endotoxin affects insecticidal specificity Biochem. J. 302 1994 611 616
    • (1994) Biochem. J. , vol.302 , pp. 611-616
    • Smith, G.P.1    Ellar, D.J.2
  • 24
    • 0029993089 scopus 로고    scopus 로고
    • Mutagenesis of three surface-exposed loops of a Bacillus thuringiensis insecticidal toxin reveals residues important for toxicity, receptor recognition and possibly membrane insertion
    • D.P. Smedley, and D.J. Ellar Mutagenesis of three surface-exposed loops of a Bacillus thuringiensis insecticidal toxin reveals residues important for toxicity, receptor recognition and possibly membrane insertion Microbiology 142 1996 1617 1624
    • (1996) Microbiology , vol.142 , pp. 1617-1624
    • Smedley, D.P.1    Ellar, D.J.2
  • 25
    • 0029869450 scopus 로고    scopus 로고
    • Functional significance of loops in the receptor binding domain of Bacillus thuringiensis CryIIIA δ-endotoxin
    • S.J. Wu, and D.H. Dean Functional significance of loops in the receptor binding domain of Bacillus thuringiensis CryIIIA δ-endotoxin J. Mol. Biol. 255 1996 628 640
    • (1996) J. Mol. Biol. , vol.255 , pp. 628-640
    • Wu, S.J.1    Dean, D.H.2
  • 26
    • 0029792870 scopus 로고    scopus 로고
    • Mutations at domain II, loop 3, of Bacillus thuringiensis CryIAa and CryIAb delta-endotoxins suggest loop 3 is involved in initial binding to lepidopteran midguts
    • F. Rajamohan, S.R. Hussain, J.A. Cotrill, F. Gould, and D.H. Dean Mutations at domain II, loop 3, of Bacillus thuringiensis CryIAa and CryIAb delta-endotoxins suggest loop 3 is involved in initial binding to lepidopteran midguts J. Biol. Chem. 271 1996 25220 25226
    • (1996) J. Biol. Chem. , vol.271 , pp. 25220-25226
    • Rajamohan, F.1    Hussain, S.R.2    Cotrill, J.A.3    Gould, F.4    Dean, D.H.5
  • 27
    • 0028846881 scopus 로고
    • Domain III exchange of Bacillus thuringiensis CryIA toxins affects binding to different gypsy moth midgut receptors
    • M.K. Lee, B.A. Young, and D.H. Dean Domain III exchange of Bacillus thuringiensis CryIA toxins affects binding to different gypsy moth midgut receptors Biochem. Biophys. Res. Commun. 216 1995 306 312
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 306-312
    • Lee, M.K.1    Young, B.A.2    Dean, D.H.3
  • 28
    • 0029930607 scopus 로고    scopus 로고
    • Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition
    • R.A. de Maagd, M.S.G. Kwa, H. van der Klei, T. Yamamoto, B. Schipper, and J.M. Vlak Domain III substitution in Bacillus thuringiensis delta-endotoxin CryIA(b) results in superior toxicity for Spodoptera exigua and altered membrane protein recognition Appl. Environ. Microbiol. 62 1996 1537 1543
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1537-1543
    • De Maagd, R.A.1    Kwa, M.S.G.2    Van Der Klei, H.3    Yamamoto, T.4    Schipper, B.5    Vlak, J.M.6
  • 29
    • 0033574601 scopus 로고    scopus 로고
    • N-acetyl galactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin
    • S.L. Burton, D.J. Ellar, J. Li, and D.J. Derbyshire N-acetyl galactosamine on the putative insect receptor aminopeptidase N is recognised by a site on the domain III lectin-like fold of a Bacillus thuringiensis insecticidal toxin J. Mol. Biol. 287 1999 1011 1022
    • (1999) J. Mol. Biol. , vol.287 , pp. 1011-1022
    • Burton, S.L.1    Ellar, D.J.2    Li, J.3    Derbyshire, D.J.4
  • 30
    • 0027359047 scopus 로고
    • Site-directed mutations in a highly conserved region of Bacillus thuringiensis δ-endotoxin affect inhibition of short circuit current across Bombyx mori midguts
    • X.J. Chen, M.K. Lee, and D.H. Dean Site-directed mutations in a highly conserved region of Bacillus thuringiensis δ-endotoxin affect inhibition of short circuit current across Bombyx mori midguts Proc. Natl Acad. Sci. USA 90 1993 9041 9045
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9041-9045
    • Chen, X.J.1    Lee, M.K.2    Dean, D.H.3
  • 31
    • 0030022109 scopus 로고    scopus 로고
    • Site-directed mutations in the third domain of Bacillus thuringiensis δ-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles
    • M.G. Wolfersberger, X.J. Chen, and D.H. Dean Site-directed mutations in the third domain of Bacillus thuringiensis δ-endotoxin CryIAa affect its ability to increase the permeability of Bombyx mori midgut brush border membrane vesicles Appl. Environ. Microbiol. 62 1996 279 282
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 279-282
    • Wolfersberger, M.G.1    Chen, X.J.2    Dean, D.H.3
  • 32
    • 0026890951 scopus 로고
    • Comparison of Bacillus thuringiensis subsp. israelensis CryIVA and CryIVB cloned toxins reveals synergism in vivo
    • C. Angsuthanasombat, N. Crickmore, and D.J. Ellar Comparison of Bacillus thuringiensis subsp. israelensis CryIVA and CryIVB cloned toxins reveals synergism in vivo FEMS Microbiol. Letters 73 1992 63 68
    • (1992) FEMS Microbiol. Letters , vol.73 , pp. 63-68
    • Angsuthanasombat, C.1    Crickmore, N.2    Ellar, D.J.3
  • 33
    • 0027490539 scopus 로고
    • Expression of cryIVA and cryIVB genes, independently or in combination, in a crystal-negative strain of Bacillus thuringiensis subsp. israelensis
    • A. Delécluse, S. Poncet, A. Klier, and G. Rapoport Expression of cryIVA and cryIVB genes, independently or in combination, in a crystal-negative strain of Bacillus thuringiensis subsp. israelensis Appl. Environ. Microbiol. 59 1993 3922 3927
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3922-3927
    • Delécluse, A.1    Poncet, S.2    Klier, A.3    Rapoport, G.4
  • 34
    • 0026425782 scopus 로고
    • Cytotoxicity of a cloned Bacillus thuringiensis subsp. israelensis CryIVB toxin to an Aedes aegypti cell line
    • C. Angsuthanasombat, N. Crickmore, and D.J. Ellar Cytotoxicity of a cloned Bacillus thuringiensis subsp. israelensis CryIVB toxin to an Aedes aegypti cell line FEMS Microbiol. Letters 83 1991 273 276
    • (1991) FEMS Microbiol. Letters , vol.83 , pp. 273-276
    • Angsuthanasombat, C.1    Crickmore, N.2    Ellar, D.J.3
  • 35
    • 0024337104 scopus 로고
    • Insecticidal crystal proteins of Bacillus thuringiensis
    • H. Höfte, and H.R. Whiteley Insecticidal crystal proteins of Bacillus thuringiensis Microbiol. Rev. 53 1989 242 255
    • (1989) Microbiol. Rev. , vol.53 , pp. 242-255
    • Höfte, H.1    Whiteley, H.R.2
  • 36
    • 0025523351 scopus 로고
    • Models for the structure and function of the Bacillus thuringiensis δ-endotoxins determined by compilational analysis
    • T.C. Hodgman, and D.J. Ellar Models for the structure and function of the Bacillus thuringiensis δ-endotoxins determined by compilational analysis J. DNA Seque. Map. 1 1990 97 106
    • (1990) J. DNA Seque. Map. , vol.1 , pp. 97-106
    • Hodgman, T.C.1    Ellar, D.J.2
  • 37
    • 0025291626 scopus 로고
    • Location of the dipteran specificity region in a lepidopteran-dipteran crystal protein from Bacillus thuringiensis
    • W.R. Widner, and H.R. Whiteley Location of the dipteran specificity region in a lepidopteran-dipteran crystal protein from Bacillus thuringiensis J. Bacteriol. 172 1990 2826 2832
    • (1990) J. Bacteriol. , vol.172 , pp. 2826-2832
    • Widner, W.R.1    Whiteley, H.R.2
  • 38
    • 0028129469 scopus 로고
    • Location of a lepidopteran specificity region in insecticidal crystal protein CryIIA from Bacillus thuringiensis
    • Y. Liang, and D.H. Dean Location of a lepidopteran specificity region in insecticidal crystal protein CryIIA from Bacillus thuringiensis Mol. Microbiol. 13 1994 569 575
    • (1994) Mol. Microbiol. , vol.13 , pp. 569-575
    • Liang, Y.1    Dean, D.H.2
  • 39
    • 0037348708 scopus 로고    scopus 로고
    • Crystallisation and preliminary X-ray diffraction studies of a mosquito-larvicidal toxin from Bacillus thuringiensis subsp. israelensis
    • P. Boonserm, D.J. Ellar, and J. Li Crystallisation and preliminary X-ray diffraction studies of a mosquito-larvicidal toxin from Bacillus thuringiensis subsp. israelensis Acta Crystallog. sect. D 59 2003 591 594
    • (2003) Acta Crystallog. Sect. D , vol.59 , pp. 591-594
    • Boonserm, P.1    Ellar, D.J.2    Li, J.3
  • 40
    • 0034479757 scopus 로고    scopus 로고
    • TOP: A new method for protein structure comparisons and similarity searches
    • G. Lu TOP: a new method for protein structure comparisons and similarity searches J. Appl. Crystallog. 33 2000 176 183
    • (2000) J. Appl. Crystallog. , vol.33 , pp. 176-183
    • Lu, G.1
  • 42
    • 0242351172 scopus 로고    scopus 로고
    • Identification of two isoforms of aminopeptidase N in Aedes aegypti larval midgut
    • K. Pootanakit, C. Angsuthanasombat, and S. Panyim Identification of two isoforms of aminopeptidase N in Aedes aegypti larval midgut J. Biochem. Mol. Biol. 36 2003 508 513
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 508-513
    • Pootanakit, K.1    Angsuthanasombat, C.2    Panyim, S.3
  • 43
    • 0030048397 scopus 로고    scopus 로고
    • Mosquitocidal activity of the Cry1C delta-endotoxin from Bacillus thuringiensis subsp. aizawai
    • G.P. Smith, J.D. Merrick, E.J. Bone, and D.J. Ellar Mosquitocidal activity of the Cry1C delta-endotoxin from Bacillus thuringiensis subsp. aizawai Appl. Environ. Microbiol. 62 1996 680 684
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 680-684
    • Smith, G.P.1    Merrick, J.D.2    Bone, E.J.3    Ellar, D.J.4
  • 44
    • 0042352393 scopus 로고    scopus 로고
    • Binding properties of Bacillus thuringiensis Cry1C δ-endotoxin to the midgut epithelial membranes of Culex pipiens
    • S. Kamauchi, M. Yamagiwa, M. Esaki, K. Otake, and H. Sakai Binding properties of Bacillus thuringiensis Cry1C δ-endotoxin to the midgut epithelial membranes of Culex pipiens Biosci. Biotechnol. Biochem. 67 2003 94 99
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 94-99
    • Kamauchi, S.1    Yamagiwa, M.2    Esaki, M.3    Otake, K.4    Sakai, H.5
  • 45
    • 0019803827 scopus 로고
    • Isolation of a protein from the parasporal crystal of Bacillus thuringiensis var. kurstaki toxic to the mosquito larva. Aedes taeniorhyncus
    • T. Yamamoto, and R.E. McLaughlin Isolation of a protein from the parasporal crystal of Bacillus thuringiensis var. kurstaki toxic to the mosquito larva. Aedes taeniorhyncus Biochem. Biophys. Res. Commun. 103 1981 414 421
    • (1981) Biochem. Biophys. Res. Commun. , vol.103 , pp. 414-421
    • Yamamoto, T.1    McLaughlin, R.E.2
  • 46
    • 0023928301 scopus 로고
    • Amino acid sequence and entomocidal activity of the P2 crystal protein. An insect toxin from Bacillus thuringiensis var. kurstaki
    • W.P. Donovan, C.C. Dencocsik, M.P. Gilbert, M.C. Gawron-Burke, R.G. Groat, and B.C. Carlton Amino acid sequence and entomocidal activity of the P2 crystal protein. An insect toxin from Bacillus thuringiensis var. kurstaki J. Biol. Chem. 263 1988 561 567
    • (1988) J. Biol. Chem. , vol.263 , pp. 561-567
    • Donovan, W.P.1    Dencocsik, C.C.2    Gilbert, M.P.3    Gawron-Burke, M.C.4    Groat, R.G.5    Carlton, B.C.6
  • 48
    • 0031416083 scopus 로고    scopus 로고
    • Host activity spectrum of the CryIIA Bacillus thuringiensis subsp. kurstaki protein. Effects on Lepidoptera, Diptera, and non-target arthropods
    • S.R. Sim Host activity spectrum of the CryIIA Bacillus thuringiensis subsp. kurstaki protein. Effects on Lepidoptera, Diptera, and non-target arthropods Southwest Entomol. 22 1997 395 404
    • (1997) Southwest Entomol. , vol.22 , pp. 395-404
    • Sim, S.R.1
  • 49
    • 0027443116 scopus 로고
    • Rendering a membrane protein soluble in water: A common packing motif in bacterial protein toxins
    • M.W. Parker, and F. Pattus Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins Trends Biochem. Sci. 18 1993 391 395
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 391-395
    • Parker, M.W.1    Pattus, F.2
  • 50
    • 0032514753 scopus 로고    scopus 로고
    • The structure and organisation within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis δ-endotoxin are consistent with an "umbrella-like" structure of the pore
    • E. Gazit, P. La Rocca, M.S.P. Sansom, and Y. Shai The structure and organisation within the membrane of the helices composing the pore-forming domain of Bacillus thuringiensis δ-endotoxin are consistent with an "umbrella-like" structure of the pore Proc. Natl Acad. Sci. USA 95 1998 12289 12294
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12289-12294
    • Gazit, E.1    La Rocca, P.2    Sansom, M.S.P.3    Shai, Y.4
  • 51
    • 0000507423 scopus 로고    scopus 로고
    • Membrane permeabilization by Bacillus thuringiensis toxins: Protein insertion and pore formation
    • A. Charles A. Delécluse C. Nielsen-Leroux Kluwer Associate Publishing Norwell, MA
    • J.-L. Schwartz, and R. Laprade Membrane permeabilization by Bacillus thuringiensis toxins: protein insertion and pore formation A. Charles A. Delécluse C. Nielsen-Leroux Entomopathogenic Bacteria: from Laboratory to Field Application 2000 Kluwer Associate Publishing Norwell, MA 1 19
    • (2000) Entomopathogenic Bacteria: From Laboratory to Field Application , pp. 1-19
    • Schwartz, J.-L.1    Laprade, R.2
  • 52
    • 0033527563 scopus 로고    scopus 로고
    • Helix 4 of Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel
    • L. Masson, B.E. Tabashnik, Y.B. Liu, R. Brousseau, and J.L. Schwartz Helix 4 of Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel J. Biol. Chem. 274 1999 31996 32000
    • (1999) J. Biol. Chem. , vol.274 , pp. 31996-32000
    • Masson, L.1    Tabashnik, B.E.2    Liu, Y.B.3    Brousseau, R.4    Schwartz, J.L.5
  • 53
    • 0032870058 scopus 로고    scopus 로고
    • Analysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis delta-endotoxin
    • A.S. Kumar, and A.I. Aronson Analysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis delta-endotoxin J. Bacteriol. 181 1999 6103 6107
    • (1999) J. Bacteriol. , vol.181 , pp. 6103-6107
    • Kumar, A.S.1    Aronson, A.I.2
  • 54
    • 0031923098 scopus 로고    scopus 로고
    • Effects on larvicidal activity of single proline substitutions in α3 or α4 of the Bacillus thuringiensis Cry4Ba toxin
    • P. Uawithya, T. Tuntitippawan, G. Katzenmeier, S. Panyim, and C. Angsuthanasombat Effects on larvicidal activity of single proline substitutions in α3 or α4 of the Bacillus thuringiensis Cry4Ba toxin Biochem. Mol. Biol. Int. 44 1998 825 832
    • (1998) Biochem. Mol. Biol. Int. , vol.44 , pp. 825-832
    • Uawithya, P.1    Tuntitippawan, T.2    Katzenmeier, G.3    Panyim, S.4    Angsuthanasombat, C.5
  • 56
    • 0037952941 scopus 로고    scopus 로고
    • Specific mutations within the α4-α5 loop of the Bacillus thuringiensis Cry4B toxin reveal a crucial role for Asn-166 and Tyr-170
    • Y. Kanintronkul, I. Sramala, G. Katzenmeier, S. Panyim, and C. Angsuthanasombat Specific mutations within the α4-α5 loop of the Bacillus thuringiensis Cry4B toxin reveal a crucial role for Asn-166 and Tyr-170 Mol. Biotechnol. 24 2003 11 20
    • (2003) Mol. Biotechnol. , vol.24 , pp. 11-20
    • Kanintronkul, Y.1    Sramala, I.2    Katzenmeier, G.3    Panyim, S.4    Angsuthanasombat, C.5
  • 57
    • 1642501561 scopus 로고    scopus 로고
    • Ion channels formed in planar lipid bilayers by the dipteran-specific Cry4B Bacillus thuringiensis toxin and its alpha1-alpha5 fragment
    • T. Puntheeranurak, P. Uawithya, L. Potvin, C. Angsuthanasombat, and J.L. Schwartz Ion channels formed in planar lipid bilayers by the dipteran-specific Cry4B Bacillus thuringiensis toxin and its alpha1-alpha5 fragment Mol. Membr. Biol. 21 2004 67 74
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 67-74
    • Puntheeranurak, T.1    Uawithya, P.2    Potvin, L.3    Angsuthanasombat, C.4    Schwartz, J.L.5
  • 58
    • 0035929648 scopus 로고    scopus 로고
    • Role of interdomain salt bridges in the pore-forming ability of the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac
    • F. Coux, V. Vachon, C. Rang, K. Moozar, L. Masson, and M. Royer Role of interdomain salt bridges in the pore-forming ability of the Bacillus thuringiensis toxins Cry1Aa and Cry1Ac J. Biol. Chem. 276 2001 35546 35551
    • (2001) J. Biol. Chem. , vol.276 , pp. 35546-35551
    • Coux, F.1    Vachon, V.2    Rang, C.3    Moozar, K.4    Masson, L.5    Royer, M.6
  • 59
    • 0024722507 scopus 로고
    • Evidence for two different types of insecticidal P2 toxins with dual specificity in Bacillus thuringiensis subspecies
    • C.N. Nicholls, W. Ahmad, and D.J. Ellar Evidence for two different types of insecticidal P2 toxins with dual specificity in Bacillus thuringiensis subspecies J. Bacteriol. 171 1989 5141 5147
    • (1989) J. Bacteriol. , vol.171 , pp. 5141-5147
    • Nicholls, C.N.1    Ahmad, W.2    Ellar, D.J.3
  • 60
    • 0024320570 scopus 로고
    • Proteolytic processing of a coleopteran-specific delta-endotoxin produced by Bacillus thuringiensis var. tenebrionis
    • J. Carroll, and D.J. Ellar Proteolytic processing of a coleopteran-specific delta-endotoxin produced by Bacillus thuringiensis var. tenebrionis Biochem. J. 261 1989 99 105
    • (1989) Biochem. J. , vol.261 , pp. 99-105
    • Carroll, J.1    Ellar, D.J.2
  • 61
    • 0027264640 scopus 로고
    • Effects on toxicity of eliminating a cleavage site in a predicted interhelical loop in Bacillus thuringiensis CryIVB δ-endotoxin
    • C. Angsuthanasombat, N. Crickmore, and D.J. Ellar Effects on toxicity of eliminating a cleavage site in a predicted interhelical loop in Bacillus thuringiensis CryIVB δ-endotoxin FEMS Microbiol. Letters 111 1993 255 262
    • (1993) FEMS Microbiol. Letters , vol.111 , pp. 255-262
    • Angsuthanasombat, C.1    Crickmore, N.2    Ellar, D.J.3
  • 62
    • 0037076528 scopus 로고    scopus 로고
    • Role of helix 3 in pore formation by the Bacillus thuringiensis insecticidal toxin Cry1A
    • V. Vachon, G. Préfontaine, F. Coux, C. Rang, L. Marceau, and L. Masson Role of helix 3 in pore formation by the Bacillus thuringiensis insecticidal toxin Cry1A Biochemistry 41 2002 6178 6184
    • (2002) Biochemistry , vol.41 , pp. 6178-6184
    • Vachon, V.1    Préfontaine, G.2    Coux, F.3    Rang, C.4    Marceau, L.5    Masson, L.6
  • 63
    • 0032976138 scopus 로고    scopus 로고
    • Aggregation of Bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles
    • A.I. Aronson, C. Geng, and L. Wu Aggregation of Bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles Appl. Environ. Microbiol. 65 1999 2503 2507
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2503-2507
    • Aronson, A.I.1    Geng, C.2    Wu, L.3
  • 64
    • 0037181168 scopus 로고    scopus 로고
    • Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin
    • I. Gomez, J. Sanchez, R. Miranda, A. Bravo, and M. Soberon Cadherin-like receptor binding facilitates proteolytic cleavage of helix alpha-1 in domain I and oligomer pre-pore formation of Bacillus thuringiensis Cry1Ab toxin FEBS Letters 513 2002 242 246
    • (2002) FEBS Letters , vol.513 , pp. 242-246
    • Gomez, I.1    Sanchez, J.2    Miranda, R.3    Bravo, A.4    Soberon, M.5
  • 65
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data
    • Daresbury Laboratory, Warrington, UK.
    • Leslie, A.G.W. (1992). Recent changes to the MOSFLM package for processing film and image plate data. In Joint CCP4 and ESRF-EACMB Newsletter on Protein Crystallography, no. 26, Daresbury Laboratory, Warrington, UK.
    • (1992) Joint CCP4 and ESRF-EACMB Newsletter on Protein Crystallography , vol.26
    • Leslie, A.G.W.1
  • 66
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 67
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • J. Navaza Implementation of molecular replacement in AMoRe Acta Crystallog. sect. D 57 2001 1367 1372
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 68
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf P.R. Evans A.G.W. Leslie SERC Daresbury Laboratory Warrington, UK
    • Z. Otwinowski Maximum likelihood refinement of heavy atom parameters W. Wolf P.R. Evans A.G.W. Leslie Isomorphous Replacement and Anomalous Scattering 1991 SERC Daresbury Laboratory Warrington, UK 80 86
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 69
    • 0002918520 scopus 로고
    • Heavy atom location using SHELXS-90
    • W. Wolf P.R. Evans A.G.W. Leslie SERC Daresbury Laboratory Warrington, UK
    • G.M. Sheldrick Heavy atom location using SHELXS-90 W. Wolf P.R. Evans A.G.W. Leslie Isomorphous Replacement and Anomalous Scattering 1991 SERC Daresbury Laboratory Warrington, UK 23 38
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 23-38
    • Sheldrick, G.M.1
  • 72
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • T.A. Jones, and S. Thirup Using known substructures in protein model building and crystallography EMBO J. 5 1986 819 822
    • (1986) EMBO J. , vol.5 , pp. 819-822
    • Jones, T.A.1    Thirup, S.2
  • 73
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron maps and the location of errors in these models
    • T.A. Jones, S. Cowan, J.-Y. Zou, and M. Kjeldgaard Improved methods for building protein models in electron maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Cowan, S.2    Zou, J.-Y.3    Kjeldgaard, M.4
  • 74
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • A.T. Brünger The free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 355 1992 472 474
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 75
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for map using phases from partial structures with errors
    • R.J. Read Improved Fourier coefficients for map using phases from partial structures with errors Acta Crystallog. sect. A 42 1986 140 149
    • (1986) Acta Crystallog. Sect. a , vol.42 , pp. 140-149
    • Read, R.J.1
  • 76
    • 0000771669 scopus 로고
    • Structure-factor probabilities for related structures
    • R.J. Read Structure-factor probabilities for related structures Acta Crystallog. sect. A 46 1990 900 912
    • (1990) Acta Crystallog. Sect. a , vol.46 , pp. 900-912
    • Read, R.J.1
  • 77
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallog. 26 1993 283 291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.3    Thornton, J.M.4
  • 78
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 79
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster 3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 80
    • 0041703058 scopus 로고    scopus 로고
    • Mutation of the hydrophobic residue on helix alpha5 of Bacillus thuringiensis Cry4B affects structural stability
    • C. Krittanai, A. Bourchookarn, W. Pathaichindachote, and S. Panyim Mutation of the hydrophobic residue on helix alpha5 of Bacillus thuringiensis Cry4B affects structural stability Protein Pept. Letters 10 2003 361 368
    • (2003) Protein Pept. Letters , vol.10 , pp. 361-368
    • Krittanai, C.1    Bourchookarn, A.2    Pathaichindachote, W.3    Panyim, S.4


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