메뉴 건너뛰기




Volumn 53, Issue 4, 2014, Pages 796-805

Structural basis for substrate specificity in ArnB. A key enzyme in the polymyxin resistance pathway of gram-negative bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL COLONIZATION; CATIONIC ANTIMICROBIAL PEPTIDES; GRAM-NEGATIVE BACTERIA; MODIFICATION MECHANISM; NEGATIVELY CHARGED; SPECIFIC INHIBITORS; SUBSTRATE SPECIFICITY; UDP-GLUCURONIC ACID;

EID: 84893695827     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4015677     Document Type: Article
Times cited : (21)

References (55)
  • 1
    • 0025285857 scopus 로고
    • Biochemistry of endotoxins
    • Raetz, C. R. (1990) Biochemistry of endotoxins Annu. Rev. Biochem. 59, 129-170
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 129-170
    • Raetz, C.R.1
  • 2
    • 84879418353 scopus 로고    scopus 로고
    • Fortifying the barrier: The impact of lipid A remodelling on bacterial pathogenesis
    • Needham, B. D. and Trent, M. S. (2013) Fortifying the barrier: the impact of lipid A remodelling on bacterial pathogenesis Nat. Rev. Microbiol. 11, 467-481
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 467-481
    • Needham, B.D.1    Trent, M.S.2
  • 3
    • 0033794504 scopus 로고    scopus 로고
    • Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium
    • Gunn, J. S., Ryan, S. S., Van Velkinburgh, J. C., Ernst, R. K., and Miller, S. I. (2000) Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica serovar typhimurium Infect. Immun. 68, 6139-6146
    • (2000) Infect. Immun. , vol.68 , pp. 6139-6146
    • Gunn, J.S.1    Ryan, S.S.2    Van Velkinburgh, J.C.3    Ernst, R.K.4    Miller, S.I.5
  • 4
    • 0034488452 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides and their multifunctional role in the immune system
    • Scott, M. G. and Hancock, R. E. (2000) Cationic antimicrobial peptides and their multifunctional role in the immune system Crit. Rev. Immunol. 20, 407-431 (Pubitemid 32106684)
    • (2000) Critical Reviews in Immunology , vol.20 , Issue.5 , pp. 407-431
    • Scott, M.G.1    Hancock, R.E.W.2
  • 5
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms Nature 415, 389-395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 6
    • 0026511839 scopus 로고
    • Antibiotic peptides as mediators of innate immunity
    • Zasloff, M. (1992) Antibiotic peptides as mediators of innate immunity Curr. Opin. Immunol. 4, 3-7
    • (1992) Curr. Opin. Immunol. , vol.4 , pp. 3-7
    • Zasloff, M.1
  • 7
    • 84892170602 scopus 로고    scopus 로고
    • Antibiotic development challenges: The various mechanisms of action of antimicrobial peptides and of bacterial resistance
    • Guilhelmelli, F., Vilela, N., Albuquerque, P., Derengowski, L. D., Silva-Pereira, I., and Kyaw, C. M. (2013) Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance Front. Microbiol. 4, 353
    • (2013) Front. Microbiol. , vol.4 , pp. 353
    • Guilhelmelli, F.1    Vilela, N.2    Albuquerque, P.3    Derengowski, L.D.4    Silva-Pereira, I.5    Kyaw, C.M.6
  • 8
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki, K. (1999) Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes Biochim. Biophys. Acta 1462, 1-10
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 9
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta 1462, 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 10
    • 0033798839 scopus 로고    scopus 로고
    • Crystallization of antimicrobial pores in membranes: Magainin and protegrin
    • Yang, L., Weiss, T. M., Lehrer, R. I., and Huang, H. W. (2000) Crystallization of antimicrobial pores in membranes: magainin and protegrin Biophys. J. 79, 2002-2009
    • (2000) Biophys. J. , vol.79 , pp. 2002-2009
    • Yang, L.1    Weiss, T.M.2    Lehrer, R.I.3    Huang, H.W.4
  • 11
    • 84872856945 scopus 로고    scopus 로고
    • Peptide antimicrobials: Cell wall as a bacterial target
    • Yount, N. Y. and Yeaman, M. R. (2013) Peptide antimicrobials: cell wall as a bacterial target Ann. N.Y. Acad. Sci. 1277, 127-138
    • (2013) Ann. N.Y. Acad. Sci. , vol.1277 , pp. 127-138
    • Yount, N.Y.1    Yeaman, M.R.2
  • 14
    • 0033584935 scopus 로고    scopus 로고
    • Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa
    • Ernst, R. K., Yi, E. C., Guo, L., Lim, K. B., Burns, J. L., Hackett, M., and Miller, S. I. (1999) Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa Science 286, 1561-1565
    • (1999) Science , vol.286 , pp. 1561-1565
    • Ernst, R.K.1    Yi, E.C.2    Guo, L.3    Lim, K.B.4    Burns, J.L.5    Hackett, M.6    Miller, S.I.7
  • 15
    • 33845938063 scopus 로고    scopus 로고
    • Differentiation and distribution of colistin- and sodium dodecyl sulfate-tolerant cells in Pseudomonas aeruginosa biofilms
    • DOI 10.1128/JB.00720-06
    • Haagensen, J. A., Klausen, M., Ernst, R. K., Miller, S. I., Folkesson, A., Tolker-Nielsen, T., and Molin, S. (2007) Differentiation and distribution of colistin- and sodium dodecyl sulfate-tolerant cells in Pseudomonas aeruginosa biofilms J. Bacteriol. 189, 28-37 (Pubitemid 46036219)
    • (2007) Journal of Bacteriology , vol.189 , Issue.1 , pp. 28-37
    • Haagensen, J.A.J.1    Klausen, M.2    Ernst, R.K.3    Miller, S.I.4    Folkesson, A.5    Tolker-Nielsen, T.6    Molin, S.7
  • 16
    • 40549126258 scopus 로고    scopus 로고
    • Tolerance to the antimicrobial peptide colistin in Pseudomonas aeruginosa biofilms is linked to metabolically active cells, and depends on the pmr and mexAB-oprM genes
    • DOI 10.1111/j.1365-2958.2008.06152.x
    • Pamp, S. J., Gjermansen, M., Johansen, H. K., and Tolker-Nielsen, T. (2008) Tolerance to the antimicrobial peptide colistin in Pseudomonas aeruginosa biofilms is linked to metabolically active cells, and depends on the pmr and mexAB-oprM genes Mol. Microbiol. 68, 223-240 (Pubitemid 351363790)
    • (2008) Molecular Microbiology , vol.68 , Issue.1 , pp. 223-240
    • Pamp, S.J.1    Gjermansen, M.2    Johansen, H.K.3    Tolker-Nielsen, T.4
  • 17
    • 0027201144 scopus 로고
    • Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two- component regulatory system with a possible role in virulence
    • Roland, K. L., Martin, L. E., Esther, C. R., and Spitznagel, J. K. (1993) Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence J. Bacteriol. 175, 4154-4164 (Pubitemid 23206910)
    • (1993) Journal of Bacteriology , vol.175 , Issue.13 , pp. 4154-4164
    • Roland, K.L.1    Martin, L.E.2    Esther, C.R.3    Spitznagel, J.K.4
  • 18
    • 0021342287 scopus 로고
    • Lipid A and resistance of Salmonella typhimurium to antimicrobial granule proteins of human neutrophil granulocytes
    • Shafer, W. M., Casey, S. G., and Spitznagel, J. K. (1984) Lipid A and resistance of Salmonella typhimurium to antimicrobial granule proteins of human neutrophil granulocytes Infect. Immun. 43, 834-838 (Pubitemid 14192834)
    • (1984) Infection and Immunity , vol.43 , Issue.3 , pp. 834-838
    • Shafer, W.M.1    Casey, S.G.2    Spitznagel, J.K.3
  • 19
    • 0031909562 scopus 로고    scopus 로고
    • PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance
    • DOI 10.1046/j.1365-2958.1998.00757.x
    • Gunn, J. S., Lim, K. B., Krueger, J., Kim, K., Guo, L., Hackett, M., and Miller, S. I. (1998) PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A modification and polymyxin resistance Mol. Microbiol. 27, 1171-1182 (Pubitemid 28137969)
    • (1998) Molecular Microbiology , vol.27 , Issue.6 , pp. 1171-1182
    • Gunn, J.S.1    Lim, K.B.2    Krueger, J.3    Kim, K.4    Guo, L.5    Hackett, M.6    Miller, S.I.7
  • 20
    • 0042591323 scopus 로고    scopus 로고
    • Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose in polymyxin-resistant mutants of Escherichia coli: An aminotransferase (ArnB) that generates UDP-4-amino-4-deoxy-L-arabinose
    • DOI 10.1074/jbc.M304043200
    • Breazeale, S. D., Ribeiro, A. A., and Raetz, C. R. H. (2003) Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose in polymyxin-resistant mutants of Escherichia coli. An aminotransferase (ArnB) that generates UDP-4-deoxy-L-arabinose J. Biol. Chem. 278, 24731-24739 (Pubitemid 37548630)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24731-24739
    • Breazeale, S.D.1    Ribeiro, A.A.2    Raetz, C.R.H.3
  • 21
    • 16844384914 scopus 로고    scopus 로고
    • A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose: Identification and function of UDP-4-deoxy-4-formamido-L-arabinose
    • DOI 10.1074/jbc.M414265200
    • Breazeale, S. D., Ribeiro, A. A., McClerren, A. L., and Raetz, C. R. (2005) A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose J. Biol. Chem. 280, 14154-14167 (Pubitemid 40517318)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 14154-14167
    • Breazeale, S.D.1    Ribeiro, A.A.2    McClerren, A.L.3    Raetz, C.R.H.4
  • 22
    • 37249025572 scopus 로고    scopus 로고
    • An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli
    • DOI 10.1074/jbc.M706172200
    • Yan, A., Guan, Z., and Raetz, C. R. (2007) An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli J. Biol. Chem. 282, 36077-36089 (Pubitemid 350277131)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 36077-36089
    • Yan, A.1    Guan, Z.2    Raetz, C.R.H.3
  • 23
    • 0035900775 scopus 로고    scopus 로고
    • An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: Induction on polymyxin-resistant mutants and role of a novel lipid-linked donor
    • Trent, M. S., Ribeiro, A. A., Lin, S., Cotter, R. J., and Raetz, C. R. H. (2001) An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor J. Biol. Chem. 276, 43122-43131
    • (2001) J. Biol. Chem. , vol.276 , pp. 43122-43131
    • Trent, M.S.1    Ribeiro, A.A.2    Lin, S.3    Cotter, R.J.4    Raetz, C.R.H.5
  • 24
    • 0029870085 scopus 로고    scopus 로고
    • Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid
    • DOI 10.1016/S0092-8674(00)81099-5
    • Smith, J. J., Travis, S. M., Greenberg, E. P., and Welsh, M. J. (1996) Cystic fibrosis airway epithelia fail to kill bacteria because of abnormal airway surface fluid Cell 85, 229-236 (Pubitemid 26118164)
    • (1996) Cell , vol.85 , Issue.2 , pp. 229-236
    • Smith, J.J.1    Travis, S.M.2    Greenberg, E.P.3    Welsh, M.J.4
  • 25
    • 33947197663 scopus 로고    scopus 로고
    • The epidemiology, pathogenesis and treatment of Pseudomonas aeruginosa infections
    • DOI 10.2165/00003495-200767030-00003
    • Driscoll, J. A., Brody, S. L., and Kollef, M. H. (2007) The epidemiology, pathogenesis and treatment of Pseudomonas aeruginosa infections Drugs 67, 351-368 (Pubitemid 46425550)
    • (2007) Drugs , vol.67 , Issue.3 , pp. 351-368
    • Driscoll, J.A.1    Brody, S.L.2    Kollef, M.H.3
  • 26
    • 0037148986 scopus 로고    scopus 로고
    • Eradication of initial Pseudomonas aeruginosa colonization in patients with cystic fibrosis
    • Griese, M., Muller, I., and Reinhardt, D. (2002) Eradication of initial Pseudomonas aeruginosa colonization in patients with cystic fibrosis Eur. J. Med. Res. 7, 79-80
    • (2002) Eur. J. Med. Res. , vol.7 , pp. 79-80
    • Griese, M.1    Muller, I.2    Reinhardt, D.3
  • 27
    • 0036736583 scopus 로고    scopus 로고
    • A randomised clinical trial of nebulised tobramycin or colistin in cystic fibrosis
    • Hodson, M. E., Gallagher, C. G., and Govan, J. R. (2002) A randomised clinical trial of nebulised tobramycin or colistin in cystic fibrosis Eur. Respir. J. 20, 658-664
    • (2002) Eur. Respir. J. , vol.20 , pp. 658-664
    • Hodson, M.E.1    Gallagher, C.G.2    Govan, J.R.3
  • 28
    • 0037117005 scopus 로고    scopus 로고
    • Early Pseudomonas aeruginosa colonisation in cystic fibrosis patients
    • Marchetti, F., Candusso, M., Faraguna, D., and Assael, B. M. (2002) Early Pseudomonas aeruginosa colonisation in cystic fibrosis patients Lancet 359, 626-627
    • (2002) Lancet , vol.359 , pp. 626-627
    • Marchetti, F.1    Candusso, M.2    Faraguna, D.3    Assael, B.M.4
  • 29
    • 44849133936 scopus 로고    scopus 로고
    • Antibiotic therapy against Pseudomonas aeruginosa in cystic fibrosis
    • Taccetti, G., Campana, S., Neri, A. S., Boni, V., and Festini, F. (2008) Antibiotic therapy against Pseudomonas aeruginosa in cystic fibrosis J. Chemother. 20, 166-169 (Pubitemid 351797054)
    • (2008) Journal of Chemotherapy , vol.20 , Issue.2 , pp. 166-169
    • Taccetti, G.1    Campana, S.2    Neri, A.S.3    Boni, V.4    Festini, F.5
  • 31
    • 6344289277 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance
    • Gatzeva-Topalova, P. Z., May, A. P., and Sousa, M. C. (2004) Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance Biochemistry 43, 13370-13379 (Pubitemid 39391137)
    • (2004) Biochemistry , vol.43 , Issue.42 , pp. 13370-13379
    • Gatzeva-Topalova, P.Z.1    May, A.P.2    Sousa, M.C.3
  • 32
    • 79953759821 scopus 로고    scopus 로고
    • IMOSFLM: A new graphical interface for diffraction-image processing with MOSFLM
    • Battye, T. G., Kontogiannis, L., Johnson, O., Powell, H. R., and Leslie, A. G. (2011) iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM Acta Crystallogr. 67, 271-281
    • (2011) Acta Crystallogr. , vol.67 , pp. 271-281
    • Battye, T.G.1    Kontogiannis, L.2    Johnson, O.3    Powell, H.R.4    Leslie, A.G.5
  • 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. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0037560879 scopus 로고    scopus 로고
    • Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori
    • DOI 10.1046/j.1365-2958.2003.03527.x
    • Schirm, M., Soo, E. C., Aubry, A. J., Austin, J., Thibault, P., and Logan, S. M. (2003) Structural, genetic and functional characterization of the flagellin glycosylation process in Helicobacter pylori Mol. Microbiol. 48, 1579-1592 (Pubitemid 36751063)
    • (2003) Molecular Microbiology , vol.48 , Issue.6 , pp. 1579-1592
    • Schirm, M.1    Soo, E.C.2    Aubry, A.J.3    Austin, J.4    Thibault, P.5    Logan, S.M.6
  • 36
    • 70349597601 scopus 로고    scopus 로고
    • Electronic Ligand Builder and Optimization Workbench (eLBOW): A tool for ligand coordinate and restraint generation
    • Moriarty, N. W., Grosse-Kunstleve, R. W., and Adams, P. D. (2009) electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generation Acta Crystallogr. 65, 1074-1080
    • (2009) Acta Crystallogr. , vol.65 , pp. 1074-1080
    • Moriarty, N.W.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3
  • 38
    • 0037169485 scopus 로고    scopus 로고
    • Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose
    • DOI 10.1074/jbc.M109377200
    • Breazeale, S. D., Ribeiro, A. A., and Raetz, C. R. H. (2002) Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L- arabinose J. Biol. Chem. 277, 2886-2896 (Pubitemid 34953322)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.4 , pp. 2886-2896
    • Breazeale, S.D.1    Ribeiro, A.A.2    Raetz, C.R.H.3
  • 39
    • 16844375735 scopus 로고    scopus 로고
    • Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance
    • DOI 10.1021/bi047384g
    • Gatzeva-Topalova, P. Z., May, A. P., and Sousa, M. C. (2005) Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance Biochemistry 44, 5328-5338 (Pubitemid 40489972)
    • (2005) Biochemistry , vol.44 , Issue.14 , pp. 5328-5338
    • Gatzeva-Topalova, P.Z.1    May, A.P.2    Sousa, M.C.3
  • 40
    • 0343851637 scopus 로고    scopus 로고
    • The manifold of vitamin B6 dependent enzymes
    • Schneider, G., Kack, H., and Lindqvist, Y. (2000) The manifold of vitamin B6 dependent enzymes Structure 8, R1-6
    • (2000) Structure , vol.8 , pp. 1-6
    • Schneider, G.1    Kack, H.2    Lindqvist, Y.3
  • 41
    • 20444377731 scopus 로고    scopus 로고
    • Structure and mechanism of ArnA: Conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance
    • DOI 10.1016/j.str.2005.03.018, PII S096921260500170X
    • Gatzeva-Topalova, P. Z., May, A. P., and Sousa, M. C. (2005) Structure and mechanism of ArnA: conformational change implies ordered dehydrogenase mechanism in key enzyme for polymyxin resistance Structure 13, 929-942 (Pubitemid 40804395)
    • (2005) Structure , vol.13 , Issue.6 , pp. 929-942
    • Gatzeva-Topalova, P.Z.1    May, A.P.2    Sousa, M.C.3
  • 42
    • 20744455042 scopus 로고    scopus 로고
    • Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis
    • DOI 10.1074/jbc.M501534200
    • Williams, G. J., Breazeale, S. D., Raetz, C. R., and Naismith, J. H. (2005) Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis J. Biol. Chem. 280, 23000-23008 (Pubitemid 40853210)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.24 , pp. 23000-23008
    • Williams, G.J.1    Breazeale, S.D.2    Raetz, C.R.H.3    Naismith, J.H.4
  • 43
    • 0032444219 scopus 로고    scopus 로고
    • 6-dependent enzymes
    • DOI 10.1016/S0959-440X(98)80096-1
    • Jansonius, J. N. (1998) Structure, evolution and action of vitamin B6-dependent enzymes Curr. Opin. Struct. Biol. 8, 759-769 (Pubitemid 29004674)
    • (1998) Current Opinion in Structural Biology , vol.8 , Issue.6 , pp. 759-769
    • Jansonius, J.N.1
  • 44
    • 0033548058 scopus 로고    scopus 로고
    • Non-proline cis peptide bonds in proteins
    • DOI 10.1006/jmbi.1998.2459
    • Jabs, A., Weiss, M. S., and Hilgenfeld, R. (1999) Non-proline cis peptide bonds in proteins J. Mol. Biol. 286, 291-304 (Pubitemid 29078413)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.1 , pp. 291-304
    • Jabs, A.1    Weiss, M.S.2    Hilgenfeld, R.3
  • 45
    • 0037674764 scopus 로고    scopus 로고
    • Campylobacter - A tale of two protein glycosylation systems
    • DOI 10.1016/S0966-842X(03)00079-9
    • Szymanski, C. M., Logan, S. M., Linton, D., and Wren, B. W. (2003) Campylobacter - a tale of two protein glycosylation systems Trends Microbiol. 11, 233-238 (Pubitemid 36645007)
    • (2003) Trends in Microbiology , vol.11 , Issue.5 , pp. 233-238
    • Szymanski, C.M.1    Logan, S.M.2    Linton, D.3    Wren, B.W.4
  • 46
    • 40149092973 scopus 로고    scopus 로고
    • GDP-perosamine synthase: Structural analysis and production of a novel trideoxysugar
    • DOI 10.1021/bi702430d
    • Cook, P. D. and Holden, H. M. (2008) GDP-perosamine synthase: structural analysis and production of a novel trideoxysugar Biochemistry 47, 2833-2840 (Pubitemid 351328834)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2833-2840
    • Cook, P.D.1    Holden, H.M.2
  • 47
    • 0016438523 scopus 로고
    • 4-Amino-4,6-dideoxy-D-mannose (D-perosamine): A component of the lipopolysaccharide of Vibrio cholerae 569B (Inaba)
    • Redmond, J. W. (1975) 4-Amino-4,6-dideoxy-D-mannose (D-perosamine): a component of the lipopolysaccharide of Vibrio cholerae 569B (Inaba) FEBS Lett. 50, 147-149
    • (1975) FEBS Lett. , vol.50 , pp. 147-149
    • Redmond, J.W.1
  • 49
    • 53249103318 scopus 로고    scopus 로고
    • Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase
    • Cook, P. D., Carney, A. E., and Holden, H. M. (2008) Accommodation of GDP-linked sugars in the active site of GDP-perosamine synthase Biochemistry 47, 10685-10693
    • (2008) Biochemistry , vol.47 , pp. 10685-10693
    • Cook, P.D.1    Carney, A.E.2    Holden, H.M.3
  • 52
    • 65649107268 scopus 로고    scopus 로고
    • Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K
    • Han, Q., Robinson, H., Cai, T., Tagle, D. A., and Li, J. (2009) Structural insight into the inhibition of human kynurenine aminotransferase I/glutamine transaminase K J. Med. Chem. 52, 2786-2793
    • (2009) J. Med. Chem. , vol.52 , pp. 2786-2793
    • Han, Q.1    Robinson, H.2    Cai, T.3    Tagle, D.A.4    Li, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.