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Volumn 56, Issue 4, 2013, Pages 1405-1417

Structural-functional studies of Burkholderia cenocepacia d-glycero-β-d-manno-heptose 7-phosphate kinase (HldA) and characterization of inhibitors with antibiotic adjuvant and antivirulence properties

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL ENZYME; DEXTRO GLYCERO BETA DEXTRO MANNO HAPTOSE 7 PHOSPHATE KINASE; DEXTRO GLYCERO BETA DEXTRO MANNO HAPTOSE 7 PHOSPHATE KINASE INHIBITOR; MAGNESIUM ION; PHOSPHOTRANSFERASE INHIBITOR; PICEATANNOL; QUERCETIN; TYRPHOSTIN; UNCLASSIFIED DRUG;

EID: 84874593935     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm301483h     Document Type: Article
Times cited : (17)

References (43)
  • 1
    • 65249146929 scopus 로고    scopus 로고
    • Multidrug resistance in bacteria
    • Nikaido, H. Multidrug resistance in bacteria Annu. Rev. Biochem. 2009, 78, 119-146
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 119-146
    • Nikaido, H.1
  • 2
    • 34249719971 scopus 로고    scopus 로고
    • New strategies for combating multidrug-resistant bacteria
    • DOI 10.1016/j.molmed.2007.04.004, PII S1471491407000810
    • Wright, G. D.; Sutherland, A. D. New strategies for combating multidrug-resistant bacteria Trends Mol. Med. 2007, 13, 260-267 (Pubitemid 46836873)
    • (2007) Trends in Molecular Medicine , vol.13 , Issue.6 , pp. 260-267
    • Wright, G.D.1    Sutherland, A.D.2
  • 3
    • 14944375311 scopus 로고    scopus 로고
    • New targets and screening approaches in antimicrobial drug discovery
    • DOI 10.1021/cr030116o
    • Brown, E. D.; Wright, G. D. New targets and screening approaches in antimicrobial drug discovery Chem. Rev. 2005, 105, 759-774 (Pubitemid 40359350)
    • (2005) Chemical Reviews , vol.105 , Issue.2 , pp. 759-774
    • Brown, E.D.1    Wright, G.D.2
  • 4
    • 79952701515 scopus 로고    scopus 로고
    • Bacterial cell wall assembly: Still an attractive antibacterial target
    • Bugg, T. D. H.; Braddick, D.; Dowson, C. G.; Roper, D. I. Bacterial cell wall assembly: still an attractive antibacterial target Trends Biotechnol. 2011, 29, 167-173
    • (2011) Trends Biotechnol. , vol.29 , pp. 167-173
    • Bugg, T.D.H.1    Braddick, D.2    Dowson, C.G.3    Roper, D.I.4
  • 5
    • 84862850350 scopus 로고    scopus 로고
    • Understanding efflux in Gram-negative bacteria: Opportunities for drug discovery
    • Schweizer, H. P. Understanding efflux in Gram-negative bacteria: opportunities for drug discovery Expert Opin. Drug Discovery 2012, 7, 633-642
    • (2012) Expert Opin. Drug Discovery , vol.7 , pp. 633-642
    • Schweizer, H.P.1
  • 6
    • 34548628774 scopus 로고    scopus 로고
    • Discovery and development of ATPase inhibitors of DNA gyrase as antibacterial agents
    • DOI 10.2174/092986707781368414
    • Oblak, M.; Kotnik, M.; Solmajer, T. Discovery and development of ATPase inhibitors of DNA gyrase as antibacterial agents Curr. Med. Chem. 2007, 14, 2033-2047 (Pubitemid 47578161)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.19 , pp. 2033-2047
    • Oblak, M.1    Kotnik, M.2    Solmajer, T.3
  • 7
    • 0037352743 scopus 로고    scopus 로고
    • Large-scale analysis of the meningococcus genome by gene distruption: Resistance to complement-mediated lysis
    • DOI 10.1101/gr.664303
    • Geoffroy, M.-C.; Floquet, S.; Métais, A.; Nassif, X.; Pelicic, V. Large-scale analysis of the meningococcus genome by gene disruption: resistance to complement-mediated lysis Genome Res. 2003, 13, 391-398 (Pubitemid 36395396)
    • (2003) Genome Research , vol.13 , Issue.3 , pp. 391-398
    • Geoffroy, M.-C.1    Floquet, S.2    Metais, A.3    Nassif, X.4    Pelicic, V.5
  • 8
    • 0027409501 scopus 로고
    • Outer membrane permeability barrier to azithromycin, clarithromycin, and roxithromycin in gram-negative enteric bacteria
    • Vaara, M. Outer membrane permeability barrier to azithromycin, clarithromycin, and roxithromycin in Gram-negative enteric bacteria Antimicrob. Agents Chemother. 1993, 37, 354-356 (Pubitemid 23046584)
    • (1993) Antimicrobial Agents and Chemotherapy , vol.37 , Issue.2 , pp. 354-356
    • Vaara, M.1
  • 9
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H. Molecular basis of bacterial outer membrane permeability Microbiol. Rev. 1985, 49, 1-32 (Pubitemid 15134118)
    • (1985) Microbiological Reviews , vol.49 , Issue.1 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 10
    • 0347479229 scopus 로고    scopus 로고
    • Molecular Basis of Bacterial Outer Membrane Permeability Revisited
    • DOI 10.1128/MMBR.67.4.593-656.2003
    • Nikaido, H. Molecular basis of bacterial outer membrane permeability revisited Microbiol. Mol. Biol. Rev. 2003, 67, 593-656 (Pubitemid 37549772)
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.4 , pp. 593-656
    • Nikaido, H.1
  • 11
    • 0035997382 scopus 로고    scopus 로고
    • Lipopolysaccharide endotoxins
    • DOI 10.1146/annurev.biochem.71.110601.135414
    • Raetz, C. R. H.; Whitfield, C. Lipopolysaccharide endotoxins Annu. Rev. Biochem. 2002, 71, 635-700 (Pubitemid 34800232)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 635-700
    • Raetz, C.R.H.1    Whitfield, C.2
  • 12
    • 39449115488 scopus 로고    scopus 로고
    • Mechanism and inhibition of LpxC: An essential zinc-dependent deacetylase of bacterial lipid A synthesis
    • DOI 10.2174/138920108783497668
    • Barb, A. W.; Zhou, P. Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis Curr. Pharm. Biotechnol. 2011, 9, 9-15 (Pubitemid 351266965)
    • (2008) Current Pharmaceutical Biotechnology , vol.9 , Issue.1 , pp. 9-15
    • Barb, A.W.1    Zhou, P.2
  • 13
    • 79952809277 scopus 로고    scopus 로고
    • New targets for antibacterial design: Kdo biosynthesis and LPS machinery transport to the cell surface
    • Cipolla, L.; Polissi, A.; Airoldi, C.; Gabrielli, L.; Merlo, S.; Nicotra, F. New targets for antibacterial design: Kdo biosynthesis and LPS machinery transport to the cell surface Curr. Med. Chem. 2011, 18, 830-852
    • (2011) Curr. Med. Chem. , vol.18 , pp. 830-852
    • Cipolla, L.1    Polissi, A.2    Airoldi, C.3    Gabrielli, L.4    Merlo, S.5    Nicotra, F.6
  • 15
    • 0036066728 scopus 로고    scopus 로고
    • Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides
    • Valvano, M. A.; Messner, P.; Kosma, P. Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides Microbiology 2002, 148, 1979-1989 (Pubitemid 34785282)
    • (2002) Microbiology , vol.148 , Issue.7 , pp. 1979-1989
    • Valvano, M.A.1    Messner, P.2    Kosma, P.3
  • 16
    • 22544462795 scopus 로고    scopus 로고
    • Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP-L-glycero-D-manno- heptose biosynthesis
    • DOI 10.1128/JB.187.15.5292-5300.2005
    • McArthur, F.; Andersson, C. E.; Loutet, S.; Mowbray, S. L.; Valvano, M. A. Functional analysis of the glycero-manno-heptose 7-phosphate kinase domain from the bifunctional HldE protein, which is involved in ADP- l -glycero- d -manno-heptose biosynthesis J. Bacteriol. 2005, 187, 5292-5300 (Pubitemid 41022948)
    • (2005) Journal of Bacteriology , vol.187 , Issue.15 , pp. 5292-5300
    • McArthur, F.1    Andersson, C.E.2    Loutet, S.3    Mowbray, S.L.4    Valvano, M.A.5
  • 17
    • 33644854257 scopus 로고    scopus 로고
    • A complete lipopolysaccharide inner core oligosaccharide is required for resistance of Burkholderia cenocepacia to antimicrobial peptides and bacterial survival in vivo
    • DOI 10.1128/JB.188.6.2073-2080.2006
    • Loutet, S. A.; Flannagan, R. S.; Kooi, C.; Sokol, P. A.; Valvano, M. A. A complete lipopolysaccharide inner core oligosaccharide is required for resistance of Burkholderia cenocepacia to antimicrobial peptides and bacterial survival in vivo J. Bacteriol. 2006, 188, 2073-2080 (Pubitemid 43376461)
    • (2006) Journal of Bacteriology , vol.188 , Issue.6 , pp. 2073-2080
    • Loutet, S.A.1    Flannagan, R.S.2    Kooi, C.3    Sokol, P.A.4    Valvano, M.A.5
  • 18
    • 41449099596 scopus 로고    scopus 로고
    • Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants
    • Taylor, P. L.; Blakely, K. M.; De Leon, G. P.; Walker, J. R.; McArthur, F.; Evdokimova, E.; Zhang, K.; Valvano, M. A.; Wright, G. D.; Junop, M. S. Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants J. Biol. Chem. 2008, 283, 2835-2845
    • (2008) J. Biol. Chem. , vol.283 , pp. 2835-2845
    • Taylor, P.L.1    Blakely, K.M.2    De Leon, G.P.3    Walker, J.R.4    McArthur, F.5    Evdokimova, E.6    Zhang, K.7    Valvano, M.A.8    Wright, G.D.9    Junop, M.S.10
  • 19
    • 77954387276 scopus 로고    scopus 로고
    • The structure of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei reveals a zinc binding site at the heart of the active site
    • Harmer, N. J. The structure of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei reveals a zinc binding site at the heart of the active site J. Mol. Biol. 2010, 400, 379-392
    • (2010) J. Mol. Biol. , vol.400 , pp. 379-392
    • Harmer, N.J.1
  • 20
    • 75749106680 scopus 로고    scopus 로고
    • Structural and kinetic characterization of the LPS biosynthetic enzyme d -alpha,beta- d -heptose-1,7-bisphosphate phosphatase (GmhB) from Escherichia coli
    • Taylor, P. L.; Sugiman-Marangos, S.; Zhang, K.; Valvano, M. A.; Wright, G. D.; Junop, M. S. Structural and kinetic characterization of the LPS biosynthetic enzyme d -alpha,beta- d -heptose-1,7-bisphosphate phosphatase (GmhB) from Escherichia coli Biochemistry 2010, 49, 1033-1041
    • (2010) Biochemistry , vol.49 , pp. 1033-1041
    • Taylor, P.L.1    Sugiman-Marangos, S.2    Zhang, K.3    Valvano, M.A.4    Wright, G.D.5    Junop, M.S.6
  • 21
    • 76749115813 scopus 로고    scopus 로고
    • Structural determinants of substrate recognition in the HAD superfamily member d -glycero- d -manno-heptose-1,7-bisphosphate phosphatase (GmhB)
    • Nguyen, H. H.; Wang, L.; Huang, H.; Peisach, E.; Dunaway-Mariano, D.; Allen, K. N. Structural determinants of substrate recognition in the HAD superfamily member d -glycero- d -manno-heptose-1,7-bisphosphate phosphatase (GmhB) Biochemistry 2010, 49, 1082-1092
    • (2010) Biochemistry , vol.49 , pp. 1082-1092
    • Nguyen, H.H.1    Wang, L.2    Huang, H.3    Peisach, E.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 22
    • 0034658405 scopus 로고    scopus 로고
    • The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: Catalysis with a twist
    • DOI 10.1016/S0969-2126(00)00128-3
    • Deacon, A. M.; Ni, Y. S.; Coleman, W. G.; Ealick, S. E. The crystal structure of ADP- l -glycero- d -mannoheptose 6-epimerase: catalysis with a twist Structure 2000, 8, 453-462 (Pubitemid 30304543)
    • (2000) Structure , vol.8 , Issue.5 , pp. 453-462
    • Deacon, A.M.1    Ni, Y.S.2    Coleman Jr., W.G.3    Ealick, S.E.4
  • 25
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork, P.; Sander, C.; Valencia, A. Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases Protein Sci. 1993, 2, 31-40 (Pubitemid 23029007)
    • (1993) Protein Science , vol.2 , Issue.1 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 26
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L.; Rosenström, P. Dali server: conservation mapping in 3D Nucleic Acids Res. 2010, 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 27
    • 0032520213 scopus 로고    scopus 로고
    • Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 A resolution: Insights into a new family of kinase structures
    • Sigrell, J. A.; Cameron, A. D.; Jones, T. A.; Mowbray, S. L. Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution: insights into a new family of kinase structures Structure 1998, 6, 183-193 (Pubitemid 28153882)
    • (1998) Structure , vol.6 , Issue.2 , pp. 183-193
    • Sigrell, J.A.1    Cameron, A.D.2    Jones, T.A.3    Mowbray, S.L.4
  • 28
    • 52549096726 scopus 로고    scopus 로고
    • Adenosine kinase and ribokinase - The RK family of proteins
    • Park, J.; Gupta, R. S. Adenosine kinase and ribokinase-the RK family of proteins Cell. Mol. Life Sci. 2008, 65, 2875-2896
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2875-2896
    • Park, J.1    Gupta, R.S.2
  • 29
    • 43449100659 scopus 로고    scopus 로고
    • A system for the construction of targeted unmarked gene deletions in the genus Burkholderia
    • DOI 10.1111/j.1462-2920.2008.01576.x
    • Flannagan, R. S.; Linn, T.; Valvano, M. A. A system for the construction of targeted unmarked gene deletions in the genus Burkholderia Environ. Microbiol. 2008, 10, 1652-1660 (Pubitemid 351670258)
    • (2008) Environmental Microbiology , vol.10 , Issue.6 , pp. 1652-1660
    • Flannagan, R.S.1    Linn, T.2    Valvano, M.A.3
  • 30
    • 33646037670 scopus 로고    scopus 로고
    • An in vitro screen of bacterial lipopolysaccharide biosynthetic enzymes identifies an inhibitor of ADP-heptose biosynthesis
    • De Leon, G. P.; Elowe, N. H.; Koteva, K. P.; Valvano, M. A.; Wright, G. D. An in vitro screen of bacterial lipopolysaccharide biosynthetic enzymes identifies an inhibitor of ADP-heptose biosynthesis Chem. Biol. 2006, 13, 437-441
    • (2006) Chem. Biol. , vol.13 , pp. 437-441
    • De Leon, G.P.1    Elowe, N.H.2    Koteva, K.P.3    Valvano, M.A.4    Wright, G.D.5
  • 31
    • 80052940681 scopus 로고    scopus 로고
    • Systematic synthesis of inhibitors of the two first enzymes of the bacterial heptose biosynthetic pathway: Towards antivirulence molecules targeting lipopolysaccharide biosynthesis
    • Durka, M.; Tikad, A.; Périon, R.; Bosco, M.; Andaloussi, M.; Floquet, S.; Malacain, E.; Moreau, F.; Oxoby, M.; Gerusz, V.; Vincent, S. P. Systematic synthesis of inhibitors of the two first enzymes of the bacterial heptose biosynthetic pathway: towards antivirulence molecules targeting lipopolysaccharide biosynthesis Chem.-Eur. J. 2011, 17, 11305-11313
    • (2011) Chem. - Eur. J. , vol.17 , pp. 11305-11313
    • Durka, M.1    Tikad, A.2    Périon, R.3    Bosco, M.4    Andaloussi, M.5    Floquet, S.6    Malacain, E.7    Moreau, F.8    Oxoby, M.9    Gerusz, V.10    Vincent, S.P.11
  • 32
    • 0345597983 scopus 로고    scopus 로고
    • Efficient chemical synthesis of both anomers of ADP L-glycero- and D-glycero-D-manno-heptopyranose
    • DOI 10.1016/S0008-6215(03)00319-7
    • Zamyatina, A.; Gronow, S.; Puchberger, M.; Graziani, A.; Hofinger, A.; Kosma, P. Efficient chemical synthesis of both anomers of ADP l -glycero- and d -glycero- d -manno-heptopyranose Carbohydr. Res. 2003, 338, 2571-2589 (Pubitemid 37509955)
    • (2003) Carbohydrate Research , vol.338 , Issue.23 , pp. 2571-2589
    • Zamyatina, A.1    Gronow, S.2    Puchberger, M.3    Graziani, A.4    Hofinger, A.5    Kosma, P.6
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z.; Minor, W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 1997, 276A, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. 1994, D50, 760-763.
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 38
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B.; Richards, F. M. The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 1971, 55, 379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 41
    • 27144454305 scopus 로고    scopus 로고
    • An expression vector containing a rhamnose-inducible promoter provides tightly regulated gene expression in Burkholderia cenocepacia
    • DOI 10.1016/j.plasmid.2005.03.004, PII S0147619X05000302
    • Cardona, S. T.; Valvano, M. A. An expression vector containing a rhamnose-inducible promoter provides tightly regulated gene expression in Burkholderia cenocepacia Plasmid 2005, 54, 219-228 (Pubitemid 41501620)
    • (2005) Plasmid , vol.54 , Issue.3 , pp. 219-228
    • Cardona, S.T.1    Valvano, M.A.2
  • 42
    • 0020536197 scopus 로고
    • Morphological heterogeneity among Salmonella lipopolysaccharide chemotypes in silver-stained polyacrylamide gels
    • Hitchcock, P. J.; Brown, T. M. Morphological heterogeneity among Salmonella lipopolysaccharide chemotypes in silver-stained polyacrylamide gels J. Bacteriol. 1983, 154, 269-277 (Pubitemid 13115445)
    • (1983) Journal of Bacteriology , vol.154 , Issue.1 , pp. 269-277
    • Hitchcock, P.J.1    Brown, T.M.2
  • 43
    • 0032829234 scopus 로고    scopus 로고
    • Genetic organization of the O7-specific lipopolysaccharide biosynthesis cluster of Escherichia coli VW187 (O7:K1)
    • Marolda, C. L.; Feldman, M. F.; Valvano, M. A. Genetic organization of the O7-specific lipopolysaccharide biosynthesis cluster of Escherichia coli VW187 (O7:K1) Microbiology 1999, 145, 2485-2495 (Pubitemid 29454366)
    • (1999) Microbiology , vol.145 , Issue.9 , pp. 2485-2495
    • Marolda, C.L.1    Feldman, M.F.2    Valvano, M.A.3


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