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Volumn 397, Issue 2, 2010, Pages 495-507

A New Scaffold of an Old Protein Fold Ensures Binding to the Bisintercalator Thiocoraline

Author keywords

bacterial resistance; bisintercalator; hydrophobic pocket; thiocoraline; tryptophan fluorescence

Indexed keywords

BACTERIAL PROTEIN; PROTEIN TIOX; QUINALDIC ACID; SCAFFOLD PROTEIN; THIOCORALINE; UNCLASSIFIED DRUG;

EID: 77349124415     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.01.053     Document Type: Article
Times cited : (21)

References (41)
  • 1
    • 0344830196 scopus 로고    scopus 로고
    • Thiocoraline, a novel depsipeptide with antitumor activity produced by a marine Micromonospora: II. Physico-chemical properties and structure determination
    • Baz J.P., Cañedo L.M., Fernández-Puentes J.L., and Elipe M.V.S. Thiocoraline, a novel depsipeptide with antitumor activity produced by a marine Micromonospora: II. Physico-chemical properties and structure determination. J. Antibiot. 50 (1997) 738-741
    • (1997) J. Antibiot. , vol.50 , pp. 738-741
    • Baz, J.P.1    Cañedo, L.M.2    Fernández-Puentes, J.L.3    Elipe, M.V.S.4
  • 2
    • 0030814840 scopus 로고    scopus 로고
    • Thiocoraline, a new depsipeptide with antitumor activity produced by a marine Micromonospora: I. Taxonomy, fermentation, isolation, and biological activities
    • Romero F., Espliego F., Baz J.P., de Quesada T.G., Grávalos D., de la Calle F., and Fernández-Puentes J.L. Thiocoraline, a new depsipeptide with antitumor activity produced by a marine Micromonospora: I. Taxonomy, fermentation, isolation, and biological activities. J. Antibiot. 50 (1997) 734-737
    • (1997) J. Antibiot. , vol.50 , pp. 734-737
    • Romero, F.1    Espliego, F.2    Baz, J.P.3    de Quesada, T.G.4    Grávalos, D.5    de la Calle, F.6    Fernández-Puentes, J.L.7
  • 3
    • 84984088842 scopus 로고
    • Stoffwechselprodukte von Actinomyceten Über die Konstitution von Echinomycin
    • Keller-Schierlein W., Mihailovic M., and Prelog V. Stoffwechselprodukte von Actinomyceten Über die Konstitution von Echinomycin. Helv. Chim. Acta 42 (1959) 305-322
    • (1959) Helv. Chim. Acta , vol.42 , pp. 305-322
    • Keller-Schierlein, W.1    Mihailovic, M.2    Prelog, V.3
  • 5
    • 9044241840 scopus 로고
    • Studies on quinoxaline antibiotics. II. Isolation and properties of quinomycins A, B and C
    • Yoshida T., Katagiri K., and Yokozawa S. Studies on quinoxaline antibiotics. II. Isolation and properties of quinomycins A, B and C. J. Antibiot. Ser. A 14 (1961) 330-334
    • (1961) J. Antibiot. Ser. A , vol.14 , pp. 330-334
    • Yoshida, T.1    Katagiri, K.2    Yokozawa, S.3
  • 7
    • 77349114240 scopus 로고
    • Studies on quinoxaline antibiotics. I. General properties and the producing strains
    • Kuroya M., Ishida N., Katagiri K., Shoji T., Yoshida T., Mayama M., et al. Studies on quinoxaline antibiotics. I. General properties and the producing strains. J. Antibiot. 14 (1961) 324-329
    • (1961) J. Antibiot. , vol.14 , pp. 324-329
    • Kuroya, M.1    Ishida, N.2    Katagiri, K.3    Shoji, T.4    Yoshida, T.5    Mayama, M.6
  • 8
    • 73049169076 scopus 로고
    • Studies on quinoxaline antibiotics: II. New antibiotics, triostins A, B and C
    • Shoji J., and Katagiri K. Studies on quinoxaline antibiotics: II. New antibiotics, triostins A, B and C. J. Antibiot. Ser. A 14 (1961) 335-339
    • (1961) J. Antibiot. Ser. A , vol.14 , pp. 335-339
    • Shoji, J.1    Katagiri, K.2
  • 9
    • 0028197474 scopus 로고
    • A new topoisomerase II inhibitor, BE-22179, produced by a streptomycete: I. Producing strain, fermentation, isolation and biological activity
    • Okada H., Suzuki H., Yoshinari T., Arakawa H., Okura A., Suda H., et al. A new topoisomerase II inhibitor, BE-22179, produced by a streptomycete: I. Producing strain, fermentation, isolation and biological activity. J. Antibiot. 47 (1994) 129-135
    • (1994) J. Antibiot. , vol.47 , pp. 129-135
    • Okada, H.1    Suzuki, H.2    Yoshinari, T.3    Arakawa, H.4    Okura, A.5    Suda, H.6
  • 10
    • 0027410004 scopus 로고
    • Sandramycin, a novel antitumor antibiotic produced by a Nocardioides sp.: II. Structure determination
    • Matson J.A., Colson K.L., Belofsky G.N., and Bleiberg B.B. Sandramycin, a novel antitumor antibiotic produced by a Nocardioides sp.: II. Structure determination. J. Antibiot. 46 (1993) 162-166
    • (1993) J. Antibiot. , vol.46 , pp. 162-166
    • Matson, J.A.1    Colson, K.L.2    Belofsky, G.N.3    Bleiberg, B.B.4
  • 11
    • 0024791787 scopus 로고
    • Sandramycin, a novel antitumor antibiotic produced by a Nocardioides sp. Production, isolation, characterization and biological properties
    • Matson J.A., and Bush J.A. Sandramycin, a novel antitumor antibiotic produced by a Nocardioides sp. Production, isolation, characterization and biological properties. J. Antibiot. 42 (1989) 1763-1767
    • (1989) J. Antibiot. , vol.42 , pp. 1763-1767
    • Matson, J.A.1    Bush, J.A.2
  • 12
    • 0034820575 scopus 로고    scopus 로고
    • SW-163C and E, novel antitumor depsipeptides produced by Streptomyces sp.: I. Taxonomy, fermentation, isolation and biological activities
    • Kurosawa K., Takahashi K., and Tsuda E. SW-163C and E, novel antitumor depsipeptides produced by Streptomyces sp.: I. Taxonomy, fermentation, isolation and biological activities. J Antibiot. (Tokyo) 54 (2001) 615-621
    • (2001) J Antibiot. (Tokyo) , vol.54 , pp. 615-621
    • Kurosawa, K.1    Takahashi, K.2    Tsuda, E.3
  • 13
    • 0034827133 scopus 로고    scopus 로고
    • SW-163C and E, novel antitumor depsipeptides produced by Streptomyces sp.: II. Structure elucidation
    • Takahashi K., Koshino H., Esumi Y., Tsuda E., and Kurosawa K. SW-163C and E, novel antitumor depsipeptides produced by Streptomyces sp.: II. Structure elucidation. J. Antibiot. (Tokyo) 54 (2001) 622-627
    • (2001) J. Antibiot. (Tokyo) , vol.54 , pp. 622-627
    • Takahashi, K.1    Koshino, H.2    Esumi, Y.3    Tsuda, E.4    Kurosawa, K.5
  • 14
    • 0035207155 scopus 로고    scopus 로고
    • SW-163A and B, novel immunosuppressants produced by Streptomyces sp.
    • Takahashi K., Tsuda E., and Kurosawa K. SW-163A and B, novel immunosuppressants produced by Streptomyces sp. J. Antibiot. (Tokyo) 54 (2001) 867-873
    • (2001) J. Antibiot. (Tokyo) , vol.54 , pp. 867-873
    • Takahashi, K.1    Tsuda, E.2    Kurosawa, K.3
  • 16
    • 67649961441 scopus 로고    scopus 로고
    • Escherichia coli allows efficient modular incorporation of newly isolated quinomycin biosynthetic enzyme into echinomycin biosynthetic pathway for rational design and synthesis of potent antibiotic unnatural natural product
    • Watanabe K., Hotta K., Nakaya M., Praseuth A.P., Wang C.C., Inada D., et al. Escherichia coli allows efficient modular incorporation of newly isolated quinomycin biosynthetic enzyme into echinomycin biosynthetic pathway for rational design and synthesis of potent antibiotic unnatural natural product. J. Am. Chem. Soc. 131 (2009) 9347-9353
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9347-9353
    • Watanabe, K.1    Hotta, K.2    Nakaya, M.3    Praseuth, A.P.4    Wang, C.C.5    Inada, D.6
  • 17
    • 0019157688 scopus 로고
    • BBM-928, a new antitumor antibiotic complex: I. Production, isolation, characterization and antitumor activity
    • Ohkuma H., Sakai F., Nishiyama Y., Ohbayashi M., Imanishi H., Konishi M., et al. BBM-928, a new antitumor antibiotic complex: I. Production, isolation, characterization and antitumor activity. J. Antibiot. 33 (1980) 1087-1097
    • (1980) J. Antibiot. , vol.33 , pp. 1087-1097
    • Ohkuma, H.1    Sakai, F.2    Nishiyama, Y.3    Ohbayashi, M.4    Imanishi, H.5    Konishi, M.6
  • 18
    • 0019168735 scopus 로고
    • BBM-928, a new antitumor antibiotic complex: II. Taxonomic studies on the producing organism
    • Tomita K., Hoshino Y., Sasahira T., and Kawaguchi H. BBM-928, a new antitumor antibiotic complex: II. Taxonomic studies on the producing organism. J. Antibiot. 33 (1980) 1098-1102
    • (1980) J. Antibiot. , vol.33 , pp. 1098-1102
    • Tomita, K.1    Hoshino, Y.2    Sasahira, T.3    Kawaguchi, H.4
  • 19
    • 0035977628 scopus 로고    scopus 로고
    • Total syntheses of thiocoraline and DE-22179 and assessment of their DNA binding and biological properties
    • Boger D.L., Ichikawa S., Tse W.C., Hedrick M.P., and Jin Q. Total syntheses of thiocoraline and DE-22179 and assessment of their DNA binding and biological properties. J. Am. Chem. Soc. 123 (2001) 561-568
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 561-568
    • Boger, D.L.1    Ichikawa, S.2    Tse, W.C.3    Hedrick, M.P.4    Jin, Q.5
  • 20
    • 33846899787 scopus 로고    scopus 로고
    • Bisintercalator natural products with potential therapeutic applications: isolation, structure determination, synthetic and biological studies
    • Dawson S., Malkinson J.P., Paumier D., and Searcey M. Bisintercalator natural products with potential therapeutic applications: isolation, structure determination, synthetic and biological studies. Nat. Prod. Rep. 24 (2007) 109-126
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 109-126
    • Dawson, S.1    Malkinson, J.P.2    Paumier, D.3    Searcey, M.4
  • 21
    • 34447520288 scopus 로고    scopus 로고
    • Antitumor activity, X-ray crystal structure, and DNA binding properties of thiocoraline A, a natural bisintercalating thiodepsipeptide
    • Negri A., Marco E., Garcia-Hernandez V., Domingo A., Llamas-Saiz A.L., Porto-Sanda S., et al. Antitumor activity, X-ray crystal structure, and DNA binding properties of thiocoraline A, a natural bisintercalating thiodepsipeptide. J. Med. Chem. 50 (2007) 3322-3333
    • (2007) J. Med. Chem. , vol.50 , pp. 3322-3333
    • Negri, A.1    Marco, E.2    Garcia-Hernandez, V.3    Domingo, A.4    Llamas-Saiz, A.L.5    Porto-Sanda, S.6
  • 23
  • 24
    • 32344437742 scopus 로고    scopus 로고
    • Deciphering the biosynthesis pathway of the antitumor thiocoraline from a marine actinomycete and its expression in two Streptomyces species
    • Lombó F., Valesca A., Castro A., de la Calle F., Braña A.F., Sánchez-Puelles J.M., et al. Deciphering the biosynthesis pathway of the antitumor thiocoraline from a marine actinomycete and its expression in two Streptomyces species. ChemBioChem 7 (2006) 366-376
    • (2006) ChemBioChem , vol.7 , pp. 366-376
    • Lombó, F.1    Valesca, A.2    Castro, A.3    de la Calle, F.4    Braña, A.F.5    Sánchez-Puelles, J.M.6
  • 25
    • 43949096904 scopus 로고    scopus 로고
    • Characterization of TioF, a tryptophan 2,3-dioxygenase involved in 3-hydroxyquinaldic acid formation during thiocoraline biosynthesis
    • Sheoran A., King A., Velasco A., Pero J.M., and Garneau-Tsodikova S. Characterization of TioF, a tryptophan 2,3-dioxygenase involved in 3-hydroxyquinaldic acid formation during thiocoraline biosynthesis. Mol. Biosyst. 4 (2008) 622-628
    • (2008) Mol. Biosyst. , vol.4 , pp. 622-628
    • Sheoran, A.1    King, A.2    Velasco, A.3    Pero, J.M.4    Garneau-Tsodikova, S.5
  • 27
    • 0034723074 scopus 로고    scopus 로고
    • The 1.5 Å crystal structure of a bleomycin resistance determinant from bleomycin-producing Streptomyces verticillus
    • Kawano Y., Kumagai T., Muta K., Matoba Y., Davies J., and Sugiyama M. The 1.5 Å crystal structure of a bleomycin resistance determinant from bleomycin-producing Streptomyces verticillus. J. Mol. Biol. 295 (2000) 915-925
    • (2000) J. Mol. Biol. , vol.295 , pp. 915-925
    • Kawano, Y.1    Kumagai, T.2    Muta, K.3    Matoba, Y.4    Davies, J.5    Sugiyama, M.6
  • 28
    • 0036651254 scopus 로고    scopus 로고
    • Molecular basis of mitomycin C resistance in Streptomyces: structure and function of the MRD protein
    • Martin T.W., Dauter Z., Devedjiev Y., Sheffield P., Jelen F., He M., et al. Molecular basis of mitomycin C resistance in Streptomyces: structure and function of the MRD protein. Structure 10 (2002) 933-942
    • (2002) Structure , vol.10 , pp. 933-942
    • Martin, T.W.1    Dauter, Z.2    Devedjiev, Y.3    Sheffield, P.4    Jelen, F.5    He, M.6
  • 29
    • 0035971192 scopus 로고    scopus 로고
    • Crystal structures of the transposon Tn5-carried bleomycin resistance determinant uncomplexed and complexed with bleomycin
    • Maruyama M., Kumagai T., Matoba Y., Hayashida M., Fujii T., Hata Y., and Sugiyama M. Crystal structures of the transposon Tn5-carried bleomycin resistance determinant uncomplexed and complexed with bleomycin. J. Biol. Chem. 276 (2001) 9992-9999
    • (2001) J. Biol. Chem. , vol.276 , pp. 9992-9999
    • Maruyama, M.1    Kumagai, T.2    Matoba, Y.3    Hayashida, M.4    Fujii, T.5    Hata, Y.6    Sugiyama, M.7
  • 30
    • 33746721635 scopus 로고    scopus 로고
    • The mitomycin C (MMC)-binding protein from MMC-producing microorganisms protects from the lethal effect of bleomycin: crystallographic analysis to elucidate the binding mode of the antibiotic to the protein
    • Danshiitsoodol N., de Pinho C.A., Matoba Y., Kumagai T., and Sugiyama M. The mitomycin C (MMC)-binding protein from MMC-producing microorganisms protects from the lethal effect of bleomycin: crystallographic analysis to elucidate the binding mode of the antibiotic to the protein. J. Mol. Biol. 360 (2006) 398-408
    • (2006) J. Mol. Biol. , vol.360 , pp. 398-408
    • Danshiitsoodol, N.1    de Pinho, C.A.2    Matoba, Y.3    Kumagai, T.4    Sugiyama, M.5
  • 31
    • 0037126848 scopus 로고    scopus 로고
    • The 1.6-Å crystal structure of the copper(II)-bound bleomycin complexed with the bleomycin-binding protein from bleomycin-producing Streptomyces verticillus
    • Sugiyama M., Kumagai T., Hayashida M., Maruyama M., and Matoba Y. The 1.6-Å crystal structure of the copper(II)-bound bleomycin complexed with the bleomycin-binding protein from bleomycin-producing Streptomyces verticillus. J. Biol. Chem. 277 (2002) 2311-2320
    • (2002) J. Biol. Chem. , vol.277 , pp. 2311-2320
    • Sugiyama, M.1    Kumagai, T.2    Hayashida, M.3    Maruyama, M.4    Matoba, Y.5
  • 32
    • 0028575322 scopus 로고
    • Characterisation by molecular cloning of two genes from Streptomyces verticillus encoding resistance to bleomycin
    • Sugiyama M., Thompson C.J., Kumagai T., Suzuki K., Deblaere R., Villarroel R., and Davies J. Characterisation by molecular cloning of two genes from Streptomyces verticillus encoding resistance to bleomycin. Gene 151 (1994) 11-16
    • (1994) Gene , vol.151 , pp. 11-16
    • Sugiyama, M.1    Thompson, C.J.2    Kumagai, T.3    Suzuki, K.4    Deblaere, R.5    Villarroel, R.6    Davies, J.7
  • 33
    • 0032463747 scopus 로고    scopus 로고
    • All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly
    • Bergdoll M., Eltis L.D., Cameron A.D., Dumas P., and Bolin J.T. All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly. Protein Sci. 7 (1998) 1661-1670
    • (1998) Protein Sci. , vol.7 , pp. 1661-1670
    • Bergdoll, M.1    Eltis, L.D.2    Cameron, A.D.3    Dumas, P.4    Bolin, J.T.5
  • 34
    • 0028244721 scopus 로고
    • Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering
    • Dumas P., Bergdoll M., Cagnon C., and Masson J.M. Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering. EMBO J. 13 (1994) 2483-2492
    • (1994) EMBO J. , vol.13 , pp. 2483-2492
    • Dumas, P.1    Bergdoll, M.2    Cagnon, C.3    Masson, J.M.4
  • 35
    • 0038648570 scopus 로고    scopus 로고
    • Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase
    • Huntley J.J., Fast W., Benkovic S.J., Wright P.E., and Dyson H.J. Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase. Protein Sci. 12 (2003) 1368-1375
    • (2003) Protein Sci. , vol.12 , pp. 1368-1375
    • Huntley, J.J.1    Fast, W.2    Benkovic, S.J.3    Wright, P.E.4    Dyson, H.J.5
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter Jr. C.W., and Sweet R.M. (Eds), Academic Press, New York, NY
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter Jr. C.W., and Sweet R.M. (Eds). Methods in Enzymology, Macromolecular Crystallography, Part A vol. 276 (1997), Academic Press, New York, NY 307-326
    • (1997) Methods in Enzymology, Macromolecular Crystallography, Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0033896691 scopus 로고    scopus 로고
    • Maximum likelihood density modification
    • Terwilliger T.C. Maximum likelihood density modification. Acta Crystallogr. Sect. D 56 (2000) 965-972
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 40
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 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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