메뉴 건너뛰기




Volumn 84, Issue 6, 2012, Pages 1165-1176

A cationic lumen in the Wzx flippase mediates anionic O-antigen subunit translocation in Pseudomonas aeruginosa PAO1

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; FLIPPASE WZX; O ANTIGEN; UNCLASSIFIED DRUG;

EID: 84865157678     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08084.x     Document Type: Article
Times cited : (37)

References (69)
  • 1
    • 34547860486 scopus 로고    scopus 로고
    • WaaL of Pseudomonas aeruginosa utilizes ATP in in vitro ligation of O antigen onto lipid A-core
    • Abeyrathne, P.D., and Lam, J.S. (2007) WaaL of Pseudomonas aeruginosa utilizes ATP in in vitro ligation of O antigen onto lipid A-core. Mol Microbiol 65: 1345-1359.
    • (2007) Mol Microbiol , vol.65 , pp. 1345-1359
    • Abeyrathne, P.D.1    Lam, J.S.2
  • 2
    • 17644381899 scopus 로고    scopus 로고
    • Functional characterization ofWaaL, a ligase associated with linking O-antigen polysaccharide to the core of Pseudomonas aeruginosa lipopolysaccharide
    • Abeyrathne, P.D., Daniels, C., Poon, K.K.H., Matewish, M.J., and Lam, J.S. (2005) Functional characterization ofWaaL, a ligase associated with linking O-antigen polysaccharide to the core of Pseudomonas aeruginosa lipopolysaccharide. J Bacteriol 187: 3002-3012.
    • (2005) J Bacteriol , vol.187 , pp. 3002-3012
    • Abeyrathne, P.D.1    Daniels, C.2    Poon, K.K.H.3    Matewish, M.J.4    Lam, J.S.5
  • 3
    • 0033613811 scopus 로고    scopus 로고
    • Membrane topology of the Rickettsia prowazekii ATP/ADP translocase revealed by novel dual pho-lac reporters
    • Alexeyev, M.F., and Winkler, H.H. (1999) Membrane topology of the Rickettsia prowazekii ATP/ADP translocase revealed by novel dual pho-lac reporters. J Mol Biol 285: 1503-1513.
    • (1999) J Mol Biol , vol.285 , pp. 1503-1513
    • Alexeyev, M.F.1    Winkler, H.H.2
  • 4
    • 79953745092 scopus 로고    scopus 로고
    • Superfolder GFP is fluorescent in oxidizing environments when targeted via the Sec translocon
    • Aronson, D.E., Costantini, L.M., and Snapp, E.L. (2011) Superfolder GFP is fluorescent in oxidizing environments when targeted via the Sec translocon. Traffic 12: 543-548.
    • (2011) Traffic , vol.12 , pp. 543-548
    • Aronson, D.E.1    Costantini, L.M.2    Snapp, E.L.3
  • 5
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: application to microtubules and the ribosome
    • Baker, N.A., Sept, D., Joseph, S., Holst, M.J., and McCammon, J.A. (2001) Electrostatics of nanosystems: application to microtubules and the ribosome. Proc Natl Acad Sci USA 98: 10037-10041.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 6
    • 0033609498 scopus 로고    scopus 로고
    • The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane
    • Braun, P., and von Heijne, G. (1999) The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane. Biochemistry 38: 9778-9782.
    • (1999) Biochemistry , vol.38 , pp. 9778-9782
    • Braun, P.1    von Heijne, G.2
  • 7
    • 0032917464 scopus 로고    scopus 로고
    • Effect of wzx (rfbX) mutations on A-band and B-band lipopolysaccharide biosynthesis in Pseudomonas aeruginosa O5
    • Burrows, L.L., and Lam, J.S. (1999) Effect of wzx (rfbX) mutations on A-band and B-band lipopolysaccharide biosynthesis in Pseudomonas aeruginosa O5. J Bacteriol 181: 973-980.
    • (1999) J Bacteriol , vol.181 , pp. 973-980
    • Burrows, L.L.1    Lam, J.S.2
  • 8
    • 0036134936 scopus 로고    scopus 로고
    • VmrA, a member of a novel class of Na+-coupled multidrug efflux pumps from Vibrio parahaemolyticus
    • Chen, J., Morita, Y., Huda, M.N., Kuroda, T., Mizushima, T., and Tsuchiya, T. (2002) VmrA, a member of a novel class of Na+-coupled multidrug efflux pumps from Vibrio parahaemolyticus. J Bacteriol 184: 572-576.
    • (2002) J Bacteriol , vol.184 , pp. 572-576
    • Chen, J.1    Morita, Y.2    Huda, M.N.3    Kuroda, T.4    Mizushima, T.5    Tsuchiya, T.6
  • 10
    • 50949087837 scopus 로고    scopus 로고
    • Membrane topology of the Salmonella enterica serovar Typhimurium Group B O-antigen translocase Wzx
    • Cunneen, M.M., and Reeves, P.R. (2008) Membrane topology of the Salmonella enterica serovar Typhimurium Group B O-antigen translocase Wzx. FEMS Microbiol Lett 287: 76-84.
    • (2008) FEMS Microbiol Lett , vol.287 , pp. 76-84
    • Cunneen, M.M.1    Reeves, P.R.2
  • 11
    • 63849263023 scopus 로고    scopus 로고
    • Pivotal roles of the outer membrane polysaccharide export and polysaccharide copolymerase protein families in export of extracellular polysaccharides in Gramnegative bacteria
    • Cuthbertson, L., Mainprize, I.L., Naismith, J.H., and Whitfield, C. (2009) Pivotal roles of the outer membrane polysaccharide export and polysaccharide copolymerase protein families in export of extracellular polysaccharides in Gramnegative bacteria. Microbiol Mol Biol Rev 73: 155-177.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 155-177
    • Cuthbertson, L.1    Mainprize, I.L.2    Naismith, J.H.3    Whitfield, C.4
  • 12
    • 0036942209 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa O-antigen chain length is determined before ligation to lipid A core
    • Daniels, C., Griffiths, C., Cowles, B., and Lam, J.S. (2002) Pseudomonas aeruginosa O-antigen chain length is determined before ligation to lipid A core. Environ Microbiol 4: 883-897.
    • (2002) Environ Microbiol , vol.4 , pp. 883-897
    • Daniels, C.1    Griffiths, C.2    Cowles, B.3    Lam, J.S.4
  • 13
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar, R.C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 14
    • 78650075360 scopus 로고    scopus 로고
    • Investigation of cation-p interactions in sugar-binding proteins
    • Elumalai, P., Rajasekaran, M., Liu, H.-L., and Chen, C. (2010) Investigation of cation-p interactions in sugar-binding proteins. Protoplasma 247: 13-24.
    • (2010) Protoplasma , vol.247 , pp. 13-24
    • Elumalai, P.1    Rajasekaran, M.2    Liu, H.-L.3    Chen, C.4
  • 15
    • 48849113878 scopus 로고    scopus 로고
    • Comparative protein structure modeling using MODELLER
    • Coligan, J.E., Dunn, B.M., Speicher, D.W., and Wingfield, P.T. (eds). New York: John Wiley & Sons.
    • Eswar, N., Webb, B., Marti-Renom, M.A., Madhusudhan, M.S., Eramian, D., Shen, M., et al. (2007) Comparative protein structure modeling using MODELLER. In Current Protocols in Protein Science. Coligan, J.E., Dunn, B.M., Speicher, D.W., and Wingfield, P.T. (eds). New York: John Wiley & Sons, pp. 2.9.1-2.9.31.
    • (2007) In Current Protocols in Protein Science
    • Eswar, N.1    Webb, B.2    Marti-Renom, M.A.3    Madhusudhan, M.S.4    Eramian, D.5    Shen, M.6
  • 16
    • 0033521024 scopus 로고    scopus 로고
    • The activity of a putative polyisoprenol-linked sugar translocase (Wzx) involved in Escherichia coli O antigen assembly is independent of the chemical structure of the O repeat
    • Feldman, M.F., Marolda, C.L., Monteiro, M.A., Perry, M.B., Parodi, A.J., and Valvano, M.A. (1999) The activity of a putative polyisoprenol-linked sugar translocase (Wzx) involved in Escherichia coli O antigen assembly is independent of the chemical structure of the O repeat. J Biol Chem 274: 35129-35138.
    • (1999) J Biol Chem , vol.274 , pp. 35129-35138
    • Feldman, M.F.1    Marolda, C.L.2    Monteiro, M.A.3    Perry, M.B.4    Parodi, A.J.5    Valvano, M.A.6
  • 17
    • 73949083478 scopus 로고    scopus 로고
    • The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters
    • Forrest, L.R., and Rudnick, G. (2009) The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters. Physiology (Bethesda) 24: 377-386.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 377-386
    • Forrest, L.R.1    Rudnick, G.2
  • 18
    • 78650297251 scopus 로고    scopus 로고
    • The structural basis of secondary active transport mechanisms
    • Forrest, L.R., Krämer, R., and Ziegler, C. (2011) The structural basis of secondary active transport mechanisms. Biochim Biophys Acta 1807: 167-188.
    • (2011) Biochim Biophys Acta , vol.1807 , pp. 167-188
    • Forrest, L.R.1    Krämer, R.2    Ziegler, C.3
  • 22
    • 77958596325 scopus 로고    scopus 로고
    • Structure of a cationbound multidrug and toxic compound extrusion transporter
    • He, X., Szewczyk, P., Karyakin, A., Evin, M., Hong, W.-X., Zhang, Q., and Chang, G. (2010) Structure of a cationbound multidrug and toxic compound extrusion transporter. Nature 467: 991-994.
    • (2010) Nature , vol.467 , pp. 991-994
    • He, X.1    Szewczyk, P.2    Karyakin, A.3    Evin, M.4    Hong, W.-X.5    Zhang, Q.6    Chang, G.7
  • 23
    • 0037165138 scopus 로고    scopus 로고
    • Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein
    • Helenius, J., Ng, D.T.W., Marolda, C.L., Walter, P., Valvano, M.A., and Aebi, M. (2002) Translocation of lipid-linked oligosaccharides across the ER membrane requires Rft1 protein. Nature 415: 447-450.
    • (2002) Nature , vol.415 , pp. 447-450
    • Helenius, J.1    Ng, D.T.W.2    Marolda, C.L.3    Walter, P.4    Valvano, M.A.5    Aebi, M.6
  • 24
    • 84857034286 scopus 로고    scopus 로고
    • Analyzing conformational changes in the transport cycle of EmrE
    • Henzler-Wildman, K. (2012) Analyzing conformational changes in the transport cycle of EmrE. Curr Opin Struct Biol 22: 38-43.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 38-43
    • Henzler-Wildman, K.1
  • 25
    • 57649229060 scopus 로고    scopus 로고
    • HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures
    • Ho, B.K., and Gruswitz, F. (2008) HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct Biol 8: 49.
    • (2008) BMC Struct Biol , vol.8 , pp. 49
    • Ho, B.K.1    Gruswitz, F.2
  • 26
    • 84860596785 scopus 로고    scopus 로고
    • The Wzx translocases for Salmonella enterica O-antigen processing have unexpected serotype specificity
    • Hong, Y., Cunneen, M.M., and Reeves, P.R. (2012) The Wzx translocases for Salmonella enterica O-antigen processing have unexpected serotype specificity. Mol Microbiol 84: 620-630.
    • (2012) Mol Microbiol , vol.84 , pp. 620-630
    • Hong, Y.1    Cunneen, M.M.2    Reeves, P.R.3
  • 27
    • 0035949635 scopus 로고    scopus 로고
    • Na+-driven multidrug efflux pump VcmA from Vibrio cholerae non-O1, a non-halophilic bacterium
    • Huda, M.N., Morita, Y., Kuroda, T., Mizushima, T., and Tsuchiya, T. (2001) Na+-driven multidrug efflux pump VcmA from Vibrio cholerae non-O1, a non-halophilic bacterium. FEMS Microbiol Lett 203: 235-239.
    • (2001) FEMS Microbiol Lett , vol.203 , pp. 235-239
    • Huda, M.N.1    Morita, Y.2    Kuroda, T.3    Mizushima, T.4    Tsuchiya, T.5
  • 28
  • 29
    • 79952152673 scopus 로고    scopus 로고
    • Membrane topology mapping of the O-antigen flippase (Wzx), polymerase (Wzy), and ligase (WaaL) from Pseudomonas aeruginosa PAO1 reveals novel domain architectures
    • Islam, S.T., Taylor, V.L., Qi, M., and Lam, J.S. (2010) Membrane topology mapping of the O-antigen flippase (Wzx), polymerase (Wzy), and ligase (WaaL) from Pseudomonas aeruginosa PAO1 reveals novel domain architectures. mBio 1: e00189-10.
    • (2010) mBio , vol.1
    • Islam, S.T.1    Taylor, V.L.2    Qi, M.3    Lam, J.S.4
  • 30
    • 79957993746 scopus 로고    scopus 로고
    • Dual conserved periplasmic loops possess essential charge characteristics that support a catch-and-release mechanism of O-antigen polymerization by Wzy in Pseudomonas aeruginosa PAO1
    • Islam, S.T., Gold, A.C., Taylor, V.L., Anderson, E.M., Ford, R.C., and Lam, J.S. (2011) Dual conserved periplasmic loops possess essential charge characteristics that support a catch-and-release mechanism of O-antigen polymerization by Wzy in Pseudomonas aeruginosa PAO1. J Biol Chem 286: 20600-20605.
    • (2011) J Biol Chem , vol.286 , pp. 20600-20605
    • Islam, S.T.1    Gold, A.C.2    Taylor, V.L.3    Anderson, E.M.4    Ford, R.C.5    Lam, J.S.6
  • 31
    • 34047151404 scopus 로고    scopus 로고
    • Improving the accuracy of transmembrane protein topology prediction using evolutionary information
    • Jones, D.T. (2007) Improving the accuracy of transmembrane protein topology prediction using evolutionary information. Bioinformatics 23: 538-544.
    • (2007) Bioinformatics , vol.23 , pp. 538-544
    • Jones, D.T.1
  • 32
    • 64549148861 scopus 로고    scopus 로고
    • iMembrane: homology-based membrane-insertion of proteins
    • Kelm, S., Shi, J., and Deane, C.M. (2009) iMembrane: homology-based membrane-insertion of proteins. Bioinformatics 25: 1086-1088.
    • (2009) Bioinformatics , vol.25 , pp. 1086-1088
    • Kelm, S.1    Shi, J.2    Deane, C.M.3
  • 33
    • 78650397484 scopus 로고    scopus 로고
    • A study of the evolution of inverted-topology repeats from LeuT-fold transporters using AlignMe
    • Khafizov, K., Staritzbichler, R., Stamm, M., and Forrest, L.R. (2010) A study of the evolution of inverted-topology repeats from LeuT-fold transporters using AlignMe. Biochemistry 49: 10702-10713.
    • (2010) Biochemistry , vol.49 , pp. 10702-10713
    • Khafizov, K.1    Staritzbichler, R.2    Stamm, M.3    Forrest, L.R.4
  • 34
    • 0028104375 scopus 로고
    • Monoclonal antibodies that distinguish inner core, outer core, and lipid A regions of Pseudomonas aeruginosa lipopolysaccharide
    • de Kievit, T.R., and Lam, J.S. (1994) Monoclonal antibodies that distinguish inner core, outer core, and lipid A regions of Pseudomonas aeruginosa lipopolysaccharide. J Bacteriol 176: 7129-7139.
    • (1994) J Bacteriol , vol.176 , pp. 7129-7139
    • de Kievit, T.R.1    Lam, J.S.2
  • 35
    • 0029037440 scopus 로고
    • Molecular cloning and characterization of the rfc gene of Pseudomonas aeruginosa (serotype O5)
    • de Kievit, T.R., Dasgupta, T., Schweizer, H., and Lam, J.S.(1995) Molecular cloning and characterization of the rfc gene of Pseudomonas aeruginosa (serotype O5). Mol Microbiol 16: 565-574.
    • (1995) Mol Microbiol , vol.16 , pp. 565-574
    • de Kievit, T.R.1    Dasgupta, T.2    Schweizer, H.3    Lam, J.S.4
  • 36
    • 34047095991 scopus 로고    scopus 로고
    • Conserved and variable structural features in the lipopolysaccharide of Pseudomonas aeruginosa
    • Knirel, Y.A., Bystrova, O.V., Kocharova, N.A., Zahringer, U., and Pier, G.B. (2006) Conserved and variable structural features in the lipopolysaccharide of Pseudomonas aeruginosa. J Endotoxin Res 12: 324-336.
    • (2006) J Endotoxin Res , vol.12 , pp. 324-336
    • Knirel, Y.A.1    Bystrova, O.V.2    Kocharova, N.A.3    Zahringer, U.4    Pier, G.B.5
  • 37
    • 0023195614 scopus 로고
    • Production and characterization of monoclonal antibodies against serotype strains of Pseudomonas aeruginosa
    • Lam, J.S., MacDonald, L.A., Lam, M.Y., Duchesne, L.G., and Southam, G.G. (1987) Production and characterization of monoclonal antibodies against serotype strains of Pseudomonas aeruginosa. Infect Immun 55: 1051-1057.
    • (1987) Infect Immun , vol.55 , pp. 1051-1057
    • Lam, J.S.1    MacDonald, L.A.2    Lam, M.Y.3    Duchesne, L.G.4    Southam, G.G.5
  • 38
    • 84865173458 scopus 로고    scopus 로고
    • Genetic and functional diversity of Pseudomonas aeruginosa lipopolysaccharide
    • Lam, J.S., Taylor, V.L., Islam, S.T., Hao, Y., and Kocíncová, D. (2011) Genetic and functional diversity of Pseudomonas aeruginosa lipopolysaccharide. Front Microbiol 2: 1-25.
    • (2011) Front Microbiol , vol.2 , pp. 1-25
    • Lam, J.S.1    Taylor, V.L.2    Islam, S.T.3    Hao, Y.4    Kocíncová, D.5
  • 39
    • 0029998771 scopus 로고    scopus 로고
    • An O-antigen processing function for Wzx (RfbX): a promising candidate for O-unit flippase
    • Liu, D., Cole, R.A., and Reeves, P.R. (1996) An O-antigen processing function for Wzx (RfbX): a promising candidate for O-unit flippase. J Bacteriol 178: 2102-2107.
    • (1996) J Bacteriol , vol.178 , pp. 2102-2107
    • Liu, D.1    Cole, R.A.2    Reeves, P.R.3
  • 40
    • 34248584513 scopus 로고    scopus 로고
    • Structure and function of transmembrane segment XII in osmosensor and osmoprotectant transporter ProP of Escherichia coli
    • Liu, F., Culham, D.E., Vernikovska, Y.I., Keates, R.A.B., Boggs, J.M., and Wood, J.M. (2007) Structure and function of transmembrane segment XII in osmosensor and osmoprotectant transporter ProP of Escherichia coli. Biochemistry 46: 5647-5655.
    • (2007) Biochemistry , vol.46 , pp. 5647-5655
    • Liu, F.1    Culham, D.E.2    Vernikovska, Y.I.3    Keates, R.A.B.4    Boggs, J.M.5    Wood, J.M.6
  • 41
    • 64549119506 scopus 로고    scopus 로고
    • Predicting helix-helix interactions from residue contacts in membrane proteins
    • Lo, A., Chiu, Y.-Y., Rødland, E.A., Lyu, P.-C., Sung, T.-Y., and Hsu, W.-L. (2009) Predicting helix-helix interactions from residue contacts in membrane proteins. Bioinformatics 25: 996-1003.
    • (2009) Bioinformatics , vol.25 , pp. 996-1003
    • Lo, A.1    Chiu, Y.-Y.2    Rødland, E.A.3    Lyu, P.-C.4    Sung, T.-Y.5    Hsu, W.-L.6
  • 42
    • 0033847562 scopus 로고    scopus 로고
    • Establishment of Pseudomonas aeruginosa infection: lessons from a versatile opportunist
    • Lyczak, J.B., Cannon, C.L., and Pier, G.B. (2000) Establishment of Pseudomonas aeruginosa infection: lessons from a versatile opportunist. Microbes Infect 2: 1051-1060.
    • (2000) Microbes Infect , vol.2 , pp. 1051-1060
    • Lyczak, J.B.1    Cannon, C.L.2    Pier, G.B.3
  • 43
    • 33847317012 scopus 로고    scopus 로고
    • Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural network
    • Malik, A., and Ahmad, S. (2007) Sequence and structural features of carbohydrate binding in proteins and assessment of predictability using a neural network. BMC Struct Biol 7: 1.
    • (2007) BMC Struct Biol , vol.7 , pp. 1
    • Malik, A.1    Ahmad, S.2
  • 44
    • 11044237547 scopus 로고    scopus 로고
    • Wzx proteins involved in biosynthesis of O antigen function in association with the first sugar of the O-specific lipopolysaccharide subunit
    • Marolda, C.L., Vicarioli, J., and Valvano, M.A. (2004) Wzx proteins involved in biosynthesis of O antigen function in association with the first sugar of the O-specific lipopolysaccharide subunit. Microbiology 150: 4095-4105.
    • (2004) Microbiology , vol.150 , pp. 4095-4105
    • Marolda, C.L.1    Vicarioli, J.2    Valvano, M.A.3
  • 45
    • 78649365640 scopus 로고    scopus 로고
    • Membrane topology and identification of critical amino acid residues in the Wzx O-antigen translocase from Escherichia coli O157:H4
    • Marolda, C.L., Li, B., Lung, M., Yang, M., Hanuszkiewicz, A., Rosales, A.R., and Valvano, M.A. (2010) Membrane topology and identification of critical amino acid residues in the Wzx O-antigen translocase from Escherichia coli O157:H4. J Bacteriol 192: 6160-6171.
    • (2010) J Bacteriol , vol.192 , pp. 6160-6171
    • Marolda, C.L.1    Li, B.2    Lung, M.3    Yang, M.4    Hanuszkiewicz, A.5    Rosales, A.R.6    Valvano, M.A.7
  • 46
    • 79951630927 scopus 로고    scopus 로고
    • Membrane topology and identification of critical amino acid residues in the Wzx O-antigen translocase from Escherichia coli O157:H7 -Erratum
    • Marolda, C.L., Li, B., Lung, M., Yang, M., Hanuszkiewicz, A., Rosales, A.R., and Valvano, M.A. (2011) Membrane topology and identification of critical amino acid residues in the Wzx O-antigen translocase from Escherichia coli O157:H7 -Erratum. J Bacteriol 193: 1291-1292.
    • (2011) J Bacteriol , vol.193 , pp. 1291-1292
    • Marolda, C.L.1    Li, B.2    Lung, M.3    Yang, M.4    Hanuszkiewicz, A.5    Rosales, A.R.6    Valvano, M.A.7
  • 47
    • 27744562013 scopus 로고    scopus 로고
    • Topological and transcriptional analysis of pssL gene product: a putative Wzx-like exopolysaccharide translocase in Rhizobium leguminosarum bv
    • Mazur, A., Marczak, M., Król, J.E., and Skorupska, A. (2005) Topological and transcriptional analysis of pssL gene product: a putative Wzx-like exopolysaccharide translocase in Rhizobium leguminosarum bv. trifolii TA1. Arch Microbiol 184: 1-10.
    • (2005) trifolii TA1. Arch Microbiol , vol.184 , pp. 1-10
    • Mazur, A.1    Marczak, M.2    Król, J.E.3    Skorupska, A.4
  • 48
    • 0034459552 scopus 로고    scopus 로고
    • NorM of Vibrio parahaemolyticus is an Na+-driven multidrug efflux pump
    • Morita, Y., Kataoka, A., Shiota, S., Mizushima, T., and Tsuchiya, T. (2000) NorM of Vibrio parahaemolyticus is an Na+-driven multidrug efflux pump. J Bacteriol 182: 6694-6697.
    • (2000) J Bacteriol , vol.182 , pp. 6694-6697
    • Morita, Y.1    Kataoka, A.2    Shiota, S.3    Mizushima, T.4    Tsuchiya, T.5
  • 49
    • 77950838852 scopus 로고    scopus 로고
    • Predicting transmembrane helix packing arrangements using residue contacts and a force-directed algorithm
    • Nugent, T., and Jones, D.T. (2010) Predicting transmembrane helix packing arrangements using residue contacts and a force-directed algorithm. PLoS Comput Biol 6: e1000714.
    • (2010) PLoS Comput Biol , vol.6
    • Nugent, T.1    Jones, D.T.2
  • 50
    • 0030627941 scopus 로고    scopus 로고
    • Improving contact predictions by the combination of correlated mutations and other sources of sequence information
    • Olmea, O., and Valencia, A. (1997) Improving contact predictions by the combination of correlated mutations and other sources of sequence information. Fold Des 2 (Suppl. 1): S25-S32.
    • (1997) Fold Des , vol.2 , Issue.SUPPL. 1
    • Olmea, O.1    Valencia, A.2
  • 51
    • 54949097750 scopus 로고    scopus 로고
    • MetaMQAP: a meta-server for the quality assessment of protein models
    • Pawlowski, M., Gajda, M., Matlak, R., and Bujnicki, J. (2008) MetaMQAP: a meta-server for the quality assessment of protein models. BMC Bioinformatics 9: 403.
    • (2008) BMC Bioinformatics , vol.9 , pp. 403
    • Pawlowski, M.1    Gajda, M.2    Matlak, R.3    Bujnicki, J.4
  • 52
    • 0035997382 scopus 로고    scopus 로고
    • Lipopolysaccharide endotoxins
    • Raetz, C.R.H., and Whitfield, C. (2002) Lipopolysaccharide endotoxins. Annu Rev Biochem 71: 635-700.
    • (2002) Annu Rev Biochem , vol.71 , pp. 635-700
    • Raetz, C.R.H.1    Whitfield, C.2
  • 53
    • 84858133323 scopus 로고    scopus 로고
    • Homology modeling of transporter proteins (carriers and ion channels
    • Orry, A.J.W., and Abagyan, R. (eds). New York: Humana Press.
    • Ravna, A.W., and Sylte, I. (2012) Homology modeling of transporter proteins (carriers and ion channels. In Homology Modeling: Methods and Protocols. Orry, A.J.W., and Abagyan, R. (eds). New York: Humana Press, pp. 281-299.
    • (2012) In Homology Modeling: Methods and Protocols , pp. 281-299
    • Ravna, A.W.1    Sylte, I.2
  • 54
    • 0038607122 scopus 로고    scopus 로고
    • Evidence that the wzxE gene of Escherichia coli K-12 encodes a protein involved in the transbilayer movement of a trisaccharide-lipid intermediate in the assembly of Enterobacterial Common Antigen
    • Rick, P.D., Barr, K., Sankaran, K., Kajimura, J., Rush, J.S., and Waechter, C.J. (2003) Evidence that the wzxE gene of Escherichia coli K-12 encodes a protein involved in the transbilayer movement of a trisaccharide-lipid intermediate in the assembly of Enterobacterial Common Antigen. J Biol Chem 278: 16534-16542.
    • (2003) J Biol Chem , vol.278 , pp. 16534-16542
    • Rick, P.D.1    Barr, K.2    Sankaran, K.3    Kajimura, J.4    Rush, J.S.5    Waechter, C.J.6
  • 55
    • 0014214365 scopus 로고
    • Direction of chain growth in polysaccharide synthesis: work on a bacterial polysaccharide suggests that elongation can occur at the 'reducing' end of growing chains
    • Robbins, P.W., Bray, D., Dankert, M., and Wright, A. (1967) Direction of chain growth in polysaccharide synthesis: work on a bacterial polysaccharide suggests that elongation can occur at the 'reducing' end of growing chains. Science 158: 1536-1542.
    • (1967) Science , vol.158 , pp. 1536-1542
    • Robbins, P.W.1    Bray, D.2    Dankert, M.3    Wright, A.4
  • 56
    • 67749089456 scopus 로고    scopus 로고
    • Suppression of Rft1 expression does not impair the transbilayer movement of Man5GlcNAc2-P-Pdolichol in sealed microsomes from yeast
    • Rush, J.S., Gao, N., Lehrman, M.A., Matveev, S., and Waechter, C.J. (2009) Suppression of Rft1 expression does not impair the transbilayer movement of Man5GlcNAc2-P-Pdolichol in sealed microsomes from yeast. J Biol Chem 284: 19835-19842.
    • (2009) J Biol Chem , vol.284 , pp. 19835-19842
    • Rush, J.S.1    Gao, N.2    Lehrman, M.A.3    Matveev, S.4    Waechter, C.J.5
  • 57
    • 2942624227 scopus 로고    scopus 로고
    • Advances in the prediction of protein targeting signals
    • Schneider, G., and Fechner, U. (2004) Advances in the prediction of protein targeting signals. Proteomics 4: 1571-1580.
    • (2004) Proteomics , vol.4 , pp. 1571-1580
    • Schneider, G.1    Fechner, U.2
  • 58
    • 84861557277 scopus 로고    scopus 로고
    • A model-structure of a periplasm-facing state of the NhaA antiporter suggests the molecular underpinnings of pH-induced conformational changes
    • doi:10.1074/jbc.M111.336446
    • Schushan, M., Rimon, A., Haliloglu, T., Forrest, L.R., Padan, E., and Ben-Tal, N. (2012) A model-structure of a periplasm-facing state of the NhaA antiporter suggests the molecular underpinnings of pH-induced conformational changes. J Biol Chem doi:10.1074/jbc.M111.336446.
    • (2012) J Biol Chem
    • Schushan, M.1    Rimon, A.2    Haliloglu, T.3    Forrest, L.R.4    Padan, E.5    Ben-Tal, N.6
  • 60
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Söding, J., Biegert, A., and Lupas, A.N. (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33: W244-W248.
    • (2005) Nucleic Acids Res , vol.33
    • Söding, J.1    Biegert, A.2    Lupas, A.N.3
  • 61
    • 16344390562 scopus 로고    scopus 로고
    • Properties of integral membrane protein structures: derivation of an implicit membrane potential
    • Ulmschneider, M.B., Sansom, M.S.P., and Di Nola, A. (2005) Properties of integral membrane protein structures: derivation of an implicit membrane potential. Proteins 59: 252-265.
    • (2005) Proteins , vol.59 , pp. 252-265
    • Ulmschneider, M.B.1    Sansom, M.S.P.2    Di Nola, A.3
  • 62
    • 77958533259 scopus 로고    scopus 로고
    • Structural biology: last of the multidrug transporters
    • van Veen, H.W. (2010) Structural biology: last of the multidrug transporters. Nature 467: 926-927.
    • (2010) Nature , vol.467 , pp. 926-927
    • van Veen, H.W.1
  • 63
    • 84155171096 scopus 로고    scopus 로고
    • The genetic and structural basis of two distinct terminal side branch residues in stewartan and amylovoran exopolysaccharides and their potential role in host adaptation
    • Wang, X., Yang, F., and von Bodman, S.B. (2012) The genetic and structural basis of two distinct terminal side branch residues in stewartan and amylovoran exopolysaccharides and their potential role in host adaptation. Mol Microbiol 83: 195-207.
    • (2012) Mol Microbiol , vol.83 , pp. 195-207
    • Wang, X.1    Yang, F.2    von Bodman, S.B.3
  • 64
    • 0029010356 scopus 로고
    • Biosynthesis of lipopolysaccharide O antigens
    • Whitfield, C. (1995) Biosynthesis of lipopolysaccharide O antigens. Trends Microbiol 3: 178-185.
    • (1995) Trends Microbiol , vol.3 , pp. 178-185
    • Whitfield, C.1
  • 65
    • 33746356503 scopus 로고    scopus 로고
    • Biosynthesis and assembly of capsular polysaccharides in Escherichia coli
    • Whitfield, C. (2006) Biosynthesis and assembly of capsular polysaccharides in Escherichia coli. Annu Rev Biochem 75: 39-68.
    • (2006) Annu Rev Biochem , vol.75 , pp. 39-68
    • Whitfield, C.1
  • 67
    • 17144398849 scopus 로고    scopus 로고
    • A structural model for the osmosensor, transporter, and osmoregulator ProP of Escherichia coli
    • Wood, J.M., Culham, D.E., Hillar, A., Vernikovska, Y.I., Liu, F., Boggs, J.M., and Keates, R.A.B. (2005) A structural model for the osmosensor, transporter, and osmoregulator ProP of Escherichia coli. Biochemistry 44: 5634-5646.
    • (2005) Biochemistry , vol.44 , pp. 5634-5646
    • Wood, J.M.1    Culham, D.E.2    Hillar, A.3    Vernikovska, Y.I.4    Liu, F.5    Boggs, J.M.6    Keates, R.A.B.7
  • 68
    • 77952491040 scopus 로고    scopus 로고
    • In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz
    • Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., et al. (2010) In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat Chem Biol 6: 418-423.
    • (2010) Nat Chem Biol , vol.6 , pp. 418-423
    • Woodward, R.1    Yi, W.2    Li, L.3    Zhao, G.4    Eguchi, H.5    Sridhar, P.R.6
  • 69
    • 22444432002 scopus 로고    scopus 로고
    • NMR study of the preferred membrane orientation of polyisoprenols (dolichol) and the impact of their complex with polyisoprenyl recognition sequence peptides on membrane structure
    • Zhou, G.-P., and Troy, F.A. (2005) NMR study of the preferred membrane orientation of polyisoprenols (dolichol) and the impact of their complex with polyisoprenyl recognition sequence peptides on membrane structure. Glycobiology 15: 347-359.
    • (2005) Glycobiology , vol.15 , pp. 347-359
    • Zhou, G.-P.1    Troy, F.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.