메뉴 건너뛰기




Volumn 10, Issue 11, 2002, Pages 1569-1580

Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: A 4-amino-4-deoxy-L-arabinose lipopolysaccharide-modifying enzyme

Author keywords

Aminoarabinose; Aminotransferase; cis peptide; Lipid A; Lipopolysaccharide; PLP

Indexed keywords

4 AMINO 4 DEOXY LEVO ARABINOSE; AMINOTRANSFERASE; ARABINOSE DERIVATIVE; BACTERIAL ENZYME; BACTERIUM LIPOPOLYSACCHARIDE; UNCLASSIFIED DRUG; CYCLOSERINE; DRUG DERIVATIVE; LIPOPOLYSACCHARIDE; PYRIDOXAMINE; PYRIDOXAMINE PHOSPHATE;

EID: 0036850945     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00879-1     Document Type: Article
Times cited : (66)

References (41)
  • 1
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov R., Janeway C.A. Innate immunity. the virtues of a nonclonal system of recognition Cell. 91:1997;295-298.
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.A.2
  • 2
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Guo L., Lim K.B., Pdouje C.M., Daniel M., Gunn J.S., Hackett M., Miller S.I. Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell. 95:1998;189-198.
    • (1998) Cell , vol.95 , pp. 189-198
    • Guo, L.1    Lim, K.B.2    Pdouje, C.M.3    Daniel, M.4    Gunn, J.S.5    Hackett, M.6    Miller, S.I.7
  • 3
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo L., Lim K.B., Gunn J.S., Bainbridge B., Darveau R.P., Hackett M., Miller S.I. Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science. 276:1997;250-253.
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 4
    • 0029809576 scopus 로고    scopus 로고
    • PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance
    • Gunn J.S., Miller S.I. PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance. J. Bacteriol. 178:1996;6857-6864.
    • (1996) J. Bacteriol. , vol.178 , pp. 6857-6864
    • Gunn, J.S.1    Miller, S.I.2
  • 5
    • 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 Velkinburg J.C., Ernst R.K., Miller S.I. 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. 68:2000;6139-6146.
    • (2000) Infect. Immun. , vol.68 , pp. 6139-6146
    • Gunn, J.S.1    Ryan, S.S.2    Van Velkinburg, J.C.3    Ernst, R.K.4    Miller, S.I.5
  • 6
    • 0033603353 scopus 로고    scopus 로고
    • 3 in Escherichia coli K12. Detection of 4-amino-4-deoxy-L-arabinose, phosphoethanolamine and palmitate
    • 3 in Escherichia coli K12. Detection of 4-amino-4-deoxy-L-arabinose, phosphoethanolamine and palmitate. J. Biol. Chem. 274:1999;18503-18514.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18503-18514
    • Zhou, Z.1    Lin, S.2    Cotter, R.J.3    Raetz, C.R.4
  • 7
    • 0032992831 scopus 로고    scopus 로고
    • The Salmonella typhi melittin resistance gene pqaB affects intracellular growth in PMA-differentiated U937 cells, polymyxin B resistance and lipopolysaccharide
    • Baker S.J., Gunn J.S., Morona R. The Salmonella typhi melittin resistance gene pqaB affects intracellular growth in PMA-differentiated U937 cells, polymyxin B resistance and lipopolysaccharide. Microbiology. 145:1999;367-378.
    • (1999) Microbiology , vol.145 , pp. 367-378
    • Baker, S.J.1    Gunn, J.S.2    Morona, R.3
  • 8
    • 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
    • Breazeale S.D., Ribeiro A.A., Raetz C.R. 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. 277:2002;2886-2896.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2886-2896
    • Breazeale, S.D.1    Ribeiro, A.A.2    Raetz, C.R.3
  • 9
    • 0035900684 scopus 로고    scopus 로고
    • Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation
    • Zhou Z., Ribeiro A.A., Lin S., Cotter R.J., Miller S.I., Raetz C.R. Lipid A modifications in polymyxin-resistant Salmonella typhimurium. PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation J. Biol. Chem. 276:2001;43111-43121.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43111-43121
    • Zhou, Z.1    Ribeiro, A.A.2    Lin, S.3    Cotter, R.J.4    Miller, S.I.5    Raetz, C.R.6
  • 10
    • 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., Raetz C.R. 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. 276:2001;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.5
  • 11
    • 0035900728 scopus 로고    scopus 로고
    • Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: Structural characterization and transfer to lipid A in the periplasm
    • Trent M.S., Ribeiro A.A., Doerrler W.T., Lin S., Cotter R.J., Raetz C.R. Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli. structural characterization and transfer to lipid A in the periplasm J. Biol. Chem. 276:2001;43132-43144.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43132-43144
    • Trent, M.S.1    Ribeiro, A.A.2    Doerrler, W.T.3    Lin, S.4    Cotter, R.J.5    Raetz, C.R.6
  • 12
    • 0029814366 scopus 로고    scopus 로고
    • Microbial pathogenesis in cystic fibrosis: Mucoid Pseudomonas aeruginosa and Burkholderia cepacia
    • Govan J.R., Deretic V. Microbial pathogenesis in cystic fibrosis. mucoid Pseudomonas aeruginosa and Burkholderia cepacia Microbiol. Rev. 60:1996;539-574.
    • (1996) Microbiol. Rev. , vol.60 , pp. 539-574
    • Govan, J.R.1    Deretic, V.2
  • 13
    • 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., Miller S.I. Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa. Science. 286:1999;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
  • 14
    • 0032444219 scopus 로고    scopus 로고
    • Structure, evolution and action of vitamin B6-dependent enzymes
    • Jansonius J.N. Structure, evolution and action of vitamin B6-dependent enzymes. Curr. Opin. Struct. Biol. 8:1998;759-769.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 759-769
    • Jansonius, J.N.1
  • 15
    • 0033520088 scopus 로고    scopus 로고
    • Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase
    • Eads J.C., Beeby M., Scapin G., Yu T.W., Floss H.G. Crystal structure of 3-amino-5-hydroxybenzoic acid (AHBA) synthase. Biochemistry. 38:1999;9840-9849.
    • (1999) Biochemistry , vol.38 , pp. 9840-9849
    • Eads, J.C.1    Beeby, M.2    Scapin, G.3    Yu, T.W.4    Floss, H.G.5
  • 16
    • 0026055156 scopus 로고
    • Analysis of the steric strain in the polypeptide backbone of protein molecules
    • Herzberg O., Moult J. Analysis of the steric strain in the polypeptide backbone of protein molecules. Proteins. 11:1991;223-229.
    • (1991) Proteins , vol.11 , pp. 223-229
    • Herzberg, O.1    Moult, J.2
  • 17
    • 0017088666 scopus 로고
    • An explanation for the rare occurrence of cis peptide units in proteins and polypeptides
    • Ramachandran G.N., Mitra A.K. An explanation for the rare occurrence of cis peptide units in proteins and polypeptides. J. Mol. Biol. 107:1976;85-92.
    • (1976) J. Mol. Biol. , vol.107 , pp. 85-92
    • Ramachandran, G.N.1    Mitra, A.K.2
  • 19
    • 0032542720 scopus 로고    scopus 로고
    • D-cycloserine inactivation of D-amino acid aminotransferase leads to a stable noncovalent protein complex with an aromatic cycloserine-PLP derivative
    • Peisach D., Chipman D.M., Van Ophem P.W., Manning J.M., Ringe D. D-cycloserine inactivation of D-amino acid aminotransferase leads to a stable noncovalent protein complex with an aromatic cycloserine-PLP derivative. J. Am. Chem. Soc. 120:1998;2268-2274.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 2268-2274
    • Peisach, D.1    Chipman, D.M.2    Van Ophem, P.W.3    Manning, J.M.4    Ringe, D.5
  • 21
    • 0031571665 scopus 로고    scopus 로고
    • Human ornithine aminotransferase complexed with L-canaline and gabaculine: Structural basis for substrate recognition
    • Shah S.A., Shen B.W., Brünger A.T. Human ornithine aminotransferase complexed with L-canaline and gabaculine. structural basis for substrate recognition Structure. 5:1997;1067-1075.
    • (1997) Structure , vol.5 , pp. 1067-1075
    • Shah, S.A.1    Shen, B.W.2    Brünger, A.T.3
  • 22
    • 0011514319 scopus 로고
    • A.E. Braunstein, ed. (New York: Academic Press)
    • Braunstein, A.E. (1973). The Enzymes, A.E. Braunstein, ed. (New York: Academic Press), pp. 440-448.
    • (1973) The Enzymes , pp. 440-448
    • Braunstein, A.E.1
  • 24
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublié S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276:1997;523-530.
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 25
    • 0033212804 scopus 로고    scopus 로고
    • The Rossmann Fourier autoindexing algorithm in MOSFLM
    • Powell H.R. The Rossmann Fourier autoindexing algorithm in MOSFLM. Acta Crystallogr. D. 55:1999;1690-1695.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1690-1695
    • Powell, H.R.1
  • 26
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 (Collaborative Computational Project Number 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project Number 4) suite. programs for protein crystallography Acta. Crystallogr. D. 50:1999;760-763.
    • (1999) Acta. Crystallogr. D , vol.50 , pp. 760-763
  • 27
    • 0033082065 scopus 로고    scopus 로고
    • Optimizing Shake-and-Bake for proteins
    • Weeks C.M., Miller R. Optimizing Shake-and-Bake for proteins. Acta Crystallogr. D. 55:1999;492-500.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 492-500
    • Weeks, C.M.1    Miller, R.2
  • 28
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • A. Part, C.W.J. Carter, & R.M. Sweet. New York: Academic Press
    • de la Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Part A., Carter C.W.J., Sweet R.M. Macromolecular Crystallography. 1997;Academic Press, New York. 472-494.pp.
    • (1997) Macromolecular Crystallography , pp. 472-494
    • De la Fortelle, E.1    Bricogne, G.2
  • 30
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:1999;156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 31
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D. 53:1997;240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 0025398721 scopus 로고
    • What if: A molecular modeling and drug design program
    • Vriend G. What if. a molecular modeling and drug design program J. Mol. Graph. 8:1990;52-56.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 34
    • 0032922193 scopus 로고    scopus 로고
    • Sfcheck: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vanguine A.A., Richelle J., Wodak S.J. Sfcheck. a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallogr. D. 55:1999;191-205.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 191-205
    • Vanguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 35
    • 0036008509 scopus 로고    scopus 로고
    • Reliable quality-control methods for protein crystal structures
    • Badger J., Hendle J. Reliable quality-control methods for protein crystal structures. Acta Crystallogr. D. 58:2002;284-291.
    • (2002) Acta Crystallogr. D , vol.58 , pp. 284-291
    • Badger, J.1    Hendle, J.2
  • 37
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L., Sander C. Mapping the protein universe. Science. 273:1996;595-602.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 38
    • 0035678319 scopus 로고    scopus 로고
    • Salmonella typhimurium outer membrane remodeling: Role in resistance to host innate immunity
    • Ernst R.K., Guina T., Miller S.M. Salmonella typhimurium outer membrane remodeling. role in resistance to host innate immunity Microbes Infect. 3:2001;1327-1334.
    • (2001) Microbes Infect. , vol.3 , pp. 1327-1334
    • Ernst, R.K.1    Guina, T.2    Miller, S.M.3
  • 39
    • 0014218378 scopus 로고
    • Gentamicin and colistin in chronic purulent bronchial infections
    • Pines A., Raafat H., Pluciniski K. Gentamicin and colistin in chronic purulent bronchial infections. BMJ. 551:1967;543-545.
    • (1967) BMJ , vol.551 , pp. 543-545
    • Pines, A.1    Raafat, H.2    Pluciniski, K.3
  • 40
    • 0023265976 scopus 로고
    • Colistin inhalation therapy in cystic fibrosis patients with chronic Pseudomonas aeruginosa lung infection
    • Jensen T., Pedersen S.S., Garne S., Heilmann C., Hoiby N., Koch C. Colistin inhalation therapy in cystic fibrosis patients with chronic Pseudomonas aeruginosa lung infection. J. Antimicrob. Chemother. 6:1987;831-838.
    • (1987) J. Antimicrob. Chemother. , vol.6 , pp. 831-838
    • Jensen, T.1    Pedersen, S.S.2    Garne, S.3    Heilmann, C.4    Hoiby, N.5    Koch, C.6
  • 41
    • 0025868478 scopus 로고
    • Prevention of chronic Pseudomonas aeruginosa colonisation in cystic fibrosis by early treatment
    • Valerius N.H., Koch C., Hoiby N. Prevention of chronic Pseudomonas aeruginosa colonisation in cystic fibrosis by early treatment. Lancet. 338:1991;725-726.
    • (1991) Lancet , vol.338 , pp. 725-726
    • Valerius, N.H.1    Koch, C.2    Hoiby, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.