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Volumn 22, Issue 7, 2013, Pages 883-892

The structure of DesR from Streptomyces venezuelae, a β-glucosidase involved in macrolide activation

Author keywords

glucosidase; Enzyme mechanism; Family 3 glycoside hydrolases; Macrolide antibiotics; Self resistance; X ray structure

Indexed keywords

BETA GLUCOSIDASE; LIGAND; MACROLIDE; PROTON;

EID: 84881306364     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2204     Document Type: Article
Times cited : (26)

References (31)
  • 2
    • 54849405130 scopus 로고    scopus 로고
    • Renaissance in antibacterial discovery from actinomycetes
    • Baltz RH (2008) Renaissance in antibacterial discovery from actinomycetes. Curr Opin Pharmacol 8:557-563.
    • (2008) Curr Opin Pharmacol , vol.8 , pp. 557-563
    • Baltz, R.H.1
  • 4
    • 0027105048 scopus 로고
    • Isolation and characterization of 10-deoxymethynolide produced by Streptomyces venezuelae
    • Lambalot RH, Cane DE (1992) Isolation and characterization of 10-deoxymethynolide produced by Streptomyces venezuelae. J Antibiot 45:1981-1982.
    • (1992) J Antibiot , vol.45 , pp. 1981-1982
    • Lambalot, R.H.1    Cane, D.E.2
  • 5
    • 0032514668 scopus 로고    scopus 로고
    • A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: Architecture of metabolic diversity
    • Xue Y, Zhao L, Liu HW, Sherman DH (1998) A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity. Proc Natl Acad Sci USA 95:12111-12116.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12111-12116
    • Xue, Y.1    Zhao, L.2    Liu, H.W.3    Sherman, D.H.4
  • 6
    • 0029857797 scopus 로고    scopus 로고
    • Microbial glycosylation of macrolide antibiotics by Streptomyces hygroscopicus ATCC 31080 and distribution of a macrolide glycosyl transferase in several Streptomyces strains
    • Sasaki J, Mizoue K, Morimoto S, Omura S (1996) Microbial glycosylation of macrolide antibiotics by Streptomyces hygroscopicus ATCC 31080 and distribution of a macrolide glycosyl transferase in several Streptomyces strains. J Antibiot 49:1110-1118.
    • (1996) J Antibiot , vol.49 , pp. 1110-1118
    • Sasaki, J.1    Mizoue, K.2    Morimoto, S.3    Omura, S.4
  • 7
    • 0026526159 scopus 로고
    • Role of glycosylation and deglycosylation in biosynthesis of and resistance to oleandomycin in the producer organism, Streptomyces antibioticus
    • Vilches C, Hernandez C, Mendez C, Salas JA (1992) Role of glycosylation and deglycosylation in biosynthesis of and resistance to oleandomycin in the producer organism, Streptomyces antibioticus. J Bacteriol 174: 161-165.
    • (1992) J Bacteriol , vol.174 , pp. 161-165
    • Vilches, C.1    Hernandez, C.2    Mendez, C.3    Salas, J.A.4
  • 8
    • 0027385134 scopus 로고
    • Characterization of a Streptomyces antibioticus gene cluster encoding a glycosyltransferase involved in oleandomycin inactivation
    • Hernandez C, Olano C, Mendez C, Salas JA (1993) Characterization of a Streptomyces antibioticus gene cluster encoding a glycosyltransferase involved in oleandomycin inactivation. Gene 134:139-140.
    • (1993) Gene , vol.134 , pp. 139-140
    • Hernandez, C.1    Olano, C.2    Mendez, C.3    Salas, J.A.4
  • 9
    • 0028270783 scopus 로고
    • Purification and characterization of an extracellular enzyme from Streptomyces antibioticus that converts inactive glycosylated oleandomycin into the active antibiotic
    • Quiros LM, Hernandez C, Salas JA (1994) Purification and characterization of an extracellular enzyme from Streptomyces antibioticus that converts inactive glycosylated oleandomycin into the active antibiotic. Eur J Biochem 222:129-135.
    • (1994) Eur J Biochem , vol.222 , pp. 129-135
    • Quiros, L.M.1    Hernandez, C.2    Salas, J.A.3
  • 10
    • 0031799094 scopus 로고    scopus 로고
    • Two glycosyltransferases and a glycosidase are involved in oleandomycin modification during its biosynthesis by Streptomyces antibioticus
    • Quiros LM, Aguirrezabalaga I, Olano C, Mendez C, Salas JA (1998) Two glycosyltransferases and a glycosidase are involved in oleandomycin modification during its biosynthesis by Streptomyces antibioticus. Mol Microbiol 28:1177-1185.
    • (1998) Mol Microbiol , vol.28 , pp. 1177-1185
    • Quiros, L.M.1    Aguirrezabalaga, I.2    Olano, C.3    Mendez, C.4    Salas, J.A.5
  • 11
    • 0346365104 scopus 로고    scopus 로고
    • Betaglucosylation as a part of self-resistance mechanism in methymycin/pikromycin producing strain Streptomyces venezuelae
    • Zhao L, Beyer NJ, Borisova SA, Liu HW (2003) Betaglucosylation as a part of self-resistance mechanism in methymycin/pikromycin producing strain Streptomyces venezuelae. Biochemistry 42:14794-14804.
    • (2003) Biochemistry , vol.42 , pp. 14794-14804
    • Zhao, L.1    Beyer, N.J.2    Borisova, S.A.3    Liu, H.W.4
  • 12
    • 0036204403 scopus 로고    scopus 로고
    • The family-3 glycoside hydrolases: From housekeeping functions to host-microbe interactions
    • Faure D (2002) The family-3 glycoside hydrolases: from housekeeping functions to host-microbe interactions. Appl Environ Microbiol 68:1485-1490.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 1485-1490
    • Faure, D.1
  • 16
    • 3242775493 scopus 로고    scopus 로고
    • The PA14 domain, a conserved all-beta domain in bacterial toxins, enzymes, adhesins and signaling molecules
    • Rigden DJ, Mello LV, Galperin MY (2004) The PA14 domain, a conserved all-beta domain in bacterial toxins, enzymes, adhesins and signaling molecules. Trends Biochem Sci 29:335-339.
    • (2004) Trends Biochem Sci , vol.29 , pp. 335-339
    • Rigden, D.J.1    Mello, L.V.2    Galperin, M.Y.3
  • 17
    • 0026800671 scopus 로고
    • X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution
    • Holden HM, Ito M, Hartshorne DJ, Rayment I (1992) X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution. J Mol Biol 227:840-851.
    • (1992) J Mol Biol , vol.227 , pp. 840-851
    • Holden, H.M.1    Ito, M.2    Hartshorne, D.J.3    Rayment, I.4
  • 18
    • 46849095804 scopus 로고    scopus 로고
    • Glycosidase inhibition by macrolide antibiotics elucidated by STD-NMR spectroscopy
    • Sadeghi-Khomami A, Lumsden MD, Jakeman DL (2008) Glycosidase inhibition by macrolide antibiotics elucidated by STD-NMR spectroscopy. Chem Biol 15: 739-749.
    • (2008) Chem Biol , vol.15 , pp. 739-749
    • Sadeghi-Khomami, A.1    Lumsden, M.D.2    Jakeman, D.L.3
  • 19
    • 0033081517 scopus 로고    scopus 로고
    • Threedimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase
    • Varghese JN, Hrmova M, Fincher GB (1999) Threedimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 7: 179-190.
    • (1999) Structure , vol.7 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 20
    • 77956642710 scopus 로고    scopus 로고
    • Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 betaglucosidase from Kluyveromyces marxianus
    • Yoshida E, Hidaka M, Fushinobu S, Koyanagi T, Minami H, Tamaki H, Kitaoka M, Katayama T, Kumagai H (2010) Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 betaglucosidase from Kluyveromyces marxianus. Biochem J 431:39-49.
    • (2010) Biochem J , vol.431 , pp. 39-49
    • Yoshida, E.1    Hidaka, M.2    Fushinobu, S.3    Koyanagi, T.4    Minami, H.5    Tamaki, H.6    Kitaoka, M.7    Katayama, T.8    Kumagai, H.9
  • 23
    • 84866672914 scopus 로고    scopus 로고
    • Development of inhibitors as research tools for carbohydrate-processing enzymes
    • Gloster TM (2012) Development of inhibitors as research tools for carbohydrate-processing enzymes. Biochem Soc Trans 40:913-928.
    • (2012) Biochem Soc Trans , vol.40 , pp. 913-928
    • Gloster, T.M.1
  • 24
    • 15744370513 scopus 로고    scopus 로고
    • Molecular structure of human galactokinase: Implications for Type II galactosemia
    • Thoden JB, Timson DJ, Reece RJ, Holden HM (2005) Molecular structure of human galactokinase: implications for Type II galactosemia. J Biol Chem 280: 9662-9670.
    • (2005) J Biol Chem , vol.280 , pp. 9662-9670
    • Thoden, J.B.1    Timson, D.J.2    Reece, R.J.3    Holden, H.M.4
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 0002583957 scopus 로고
    • DM:' An automated procedure for phase improvement by density modification
    • Cowtan K (1994) 'DM:' an automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newslett Prot Cryst 31:34-38.
    • (1994) Joint CCP4 ESF-EACBM Newslett Prot Cryst , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 29
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Cryst D60:2126-2132.
    • (2004) Acta Cryst , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximumlikelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximumlikelihood method. Acta Cryst D53:240-255.
    • (1997) Acta Cryst , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 0027169515 scopus 로고
    • Mainchain bond lengths and bond angles in protein structures
    • Laskowski RA, Moss DS, Thornton JM (1993) Mainchain bond lengths and bond angles in protein structures. J Mol Biol 231:1049-1067.
    • (1993) J Mol Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.