메뉴 건너뛰기




Volumn 7, Issue 5, 2011, Pages

A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins

Author keywords

[No Author keywords available]

Indexed keywords

OUTER MEMBRANE PROTEIN; PROTEIN DERIVATIVE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG; VIRB7 PROTEIN; VIRB9 PROTEIN; CARRIER PROTEIN; LIPOPROTEIN; VIRULENCE FACTOR;

EID: 79958062185     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002031     Document Type: Article
Times cited : (56)

References (89)
  • 1
    • 60849116153 scopus 로고    scopus 로고
    • Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology
    • Tseng TT, Tyler BM, Setubal JC, (2009) Protein secretion systems in bacterial-host associations, and their description in the Gene Ontology. BMC Microbiol 9 (Suppl 1): S2.
    • (2009) BMC Microbiol , vol.9 , Issue.SUPPL. 1
    • Tseng, T.T.1    Tyler, B.M.2    Setubal, J.C.3
  • 3
    • 55749108735 scopus 로고    scopus 로고
    • Type IV secretion systems: tools of bacterial horizontal gene transfer and virulence
    • Juhas M, Crook DW, Hood DW, (2008) Type IV secretion systems: tools of bacterial horizontal gene transfer and virulence. Cell Microbiol 10: 2377-2386.
    • (2008) Cell Microbiol , vol.10 , pp. 2377-2386
    • Juhas, M.1    Crook, D.W.2    Hood, D.W.3
  • 4
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • Backert S, Meyer TF, (2006) Type IV secretion systems and their effectors in bacterial pathogenesis. Curr Opin Microbiol 9: 207-217.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 5
    • 34547217380 scopus 로고    scopus 로고
    • Effector proteins translocated by Legionella pneumophila: strength in numbers
    • Ninio S, Roy CR, (2007) Effector proteins translocated by Legionella pneumophila: strength in numbers. Trends Microbiol 15: 372-380.
    • (2007) Trends Microbiol , vol.15 , pp. 372-380
    • Ninio, S.1    Roy, C.R.2
  • 6
    • 59849120333 scopus 로고    scopus 로고
    • Virulence factor secretion and translocation by Bordetella species
    • Shrivastava R, Miller JF, (2009) Virulence factor secretion and translocation by Bordetella species. Curr Opin Microbiol 12: 88-93.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 88-93
    • Shrivastava, R.1    Miller, J.F.2
  • 7
    • 60049089360 scopus 로고    scopus 로고
    • Coxiella type IV secretion and cellular microbiology
    • Voth DE, Heinzen RA, (2009) Coxiella type IV secretion and cellular microbiology. Curr Opin Microbiol 12: 74-80.
    • (2009) Curr Opin Microbiol , vol.12 , pp. 74-80
    • Voth, D.E.1    Heinzen, R.A.2
  • 8
    • 47549106865 scopus 로고    scopus 로고
    • Infection-associated type IV secretion systems of Bartonella and their diverse roles in host cell interaction
    • Dehio C, (2008) Infection-associated type IV secretion systems of Bartonella and their diverse roles in host cell interaction. Cell Microbiol 10: 1591-1598.
    • (2008) Cell Microbiol , vol.10 , pp. 1591-1598
    • Dehio, C.1
  • 9
    • 32644435882 scopus 로고    scopus 로고
    • Surviving inside a macrophage: the many ways of Brucella
    • Celli J, (2006) Surviving inside a macrophage: the many ways of Brucella. Res Microbiol 157: 93-98.
    • (2006) Res Microbiol , vol.157 , pp. 93-98
    • Celli, J.1
  • 10
    • 47549090077 scopus 로고    scopus 로고
    • Role of type IV secretion in Helicobacter pylori pathogenesis
    • Backert S, Selbach M, (2008) Role of type IV secretion in Helicobacter pylori pathogenesis. Cell Microbiol 10: 1573-1581.
    • (2008) Cell Microbiol , vol.10 , pp. 1573-1581
    • Backert, S.1    Selbach, M.2
  • 11
    • 33751179227 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens and plant cell interactions and activities required for interkingdom macromolecular transfer
    • McCullen CA, Binns AN, (2006) Agrobacterium tumefaciens and plant cell interactions and activities required for interkingdom macromolecular transfer. Annu Rev Cell Dev Biol 22: 101-127.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 101-127
    • McCullen, C.A.1    Binns, A.N.2
  • 13
    • 0037681624 scopus 로고    scopus 로고
    • Xanthomonas citri: breaking the surface
    • Brunings AM, Gabriel DW, (2003) Xanthomonas citri: breaking the surface. Mol Plant Pathol 4: 141-157.
    • (2003) Mol Plant Pathol , vol.4 , pp. 141-157
    • Brunings, A.M.1    Gabriel, D.W.2
  • 14
    • 0037161811 scopus 로고    scopus 로고
    • Comparison of the genomes of two Xanthomonas pathogens with differing host specificities
    • da Silva AC, Ferro JA, Reinach FC, Farah CS, Furlan LR, et al. (2002) Comparison of the genomes of two Xanthomonas pathogens with differing host specificities. Nature 417: 459-463.
    • (2002) Nature , vol.417 , pp. 459-463
    • da Silva, A.C.1    Ferro, J.A.2    Reinach, F.C.3    Farah, C.S.4    Furlan, L.R.5
  • 15
    • 15144362149 scopus 로고    scopus 로고
    • Identification of new protein-protein interactions involving the products of the chromosome- and plasmid-encoded type IV secretion loci of the phytopathogen Xanthomonas axonopodis pv. citri
    • Alegria MC, Souza DP, Andrade MO, Docena C, Khater L, et al. (2005) Identification of new protein-protein interactions involving the products of the chromosome- and plasmid-encoded type IV secretion loci of the phytopathogen Xanthomonas axonopodis pv. citri. J Bacteriol 187: 2315-2325.
    • (2005) J Bacteriol , vol.187 , pp. 2315-2325
    • Alegria, M.C.1    Souza, D.P.2    Andrade, M.O.3    Docena, C.4    Khater, L.5
  • 16
    • 22344455805 scopus 로고    scopus 로고
    • Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris
    • Qian W, Jia Y, Ren SX, He YQ, Feng JX, et al. (2005) Comparative and functional genomic analyses of the pathogenicity of phytopathogen Xanthomonas campestris pv. campestris. Genome Res 15: 757-767.
    • (2005) Genome Res , vol.15 , pp. 757-767
    • Qian, W.1    Jia, Y.2    Ren, S.X.3    He, Y.Q.4    Feng, J.X.5
  • 17
    • 39649106315 scopus 로고    scopus 로고
    • The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis
    • Vorholter FJ, Schneiker S, Goesmann A, Krause L, Bekel T, et al. (2008) The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis. J Biotechnol 134: 33-45.
    • (2008) J Biotechnol , vol.134 , pp. 33-45
    • Vorholter, F.J.1    Schneiker, S.2    Goesmann, A.3    Krause, L.4    Bekel, T.5
  • 18
    • 75449104484 scopus 로고    scopus 로고
    • The complete genome sequence of Xanthomonas albilineans provides new insights into the reductive genome evolution of the xylem-limited Xanthomonadaceae
    • Pieretti I, Royer M, Barbe V, Carrere S, Koebnik R, et al. (2009) The complete genome sequence of Xanthomonas albilineans provides new insights into the reductive genome evolution of the xylem-limited Xanthomonadaceae. BMC Genomics 10: 616.
    • (2009) BMC Genomics , vol.10 , pp. 616
    • Pieretti, I.1    Royer, M.2    Barbe, V.3    Carrere, S.4    Koebnik, R.5
  • 19
    • 77956033435 scopus 로고    scopus 로고
    • Genome-wide sequencing data reveals virulence factors implicated in banana Xanthomonas wilt
    • Studholme DJ, Kemen E, Maclean D, Schornack S, Aritua V, et al. (2010) Genome-wide sequencing data reveals virulence factors implicated in banana Xanthomonas wilt. FEMS Microbiol Lett 310: 182-192.
    • (2010) FEMS Microbiol Lett , vol.310 , pp. 182-192
    • Studholme, D.J.1    Kemen, E.2    Maclean, D.3    Schornack, S.4    Aritua, V.5
  • 20
    • 46249094919 scopus 로고    scopus 로고
    • The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants
    • Crossman LC, Gould VC, Dow JM, Vernikos GS, Okazaki A, et al. (2008) The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants. Genome Biol 9: R74.
    • (2008) Genome Biol , vol.9
    • Crossman, L.C.1    Gould, V.C.2    Dow, J.M.3    Vernikos, G.S.4    Okazaki, A.5
  • 22
    • 27144440067 scopus 로고    scopus 로고
    • Insights into genome plasticity and pathogenicity of the plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence
    • Thieme F, Koebnik R, Bekel T, Berger C, Boch J, et al. (2005) Insights into genome plasticity and pathogenicity of the plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence. J Bacteriol 187: 7254-7266.
    • (2005) J Bacteriol , vol.187 , pp. 7254-7266
    • Thieme, F.1    Koebnik, R.2    Bekel, T.3    Berger, C.4    Boch, J.5
  • 23
    • 13744253238 scopus 로고    scopus 로고
    • The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice
    • Lee BM, Park YJ, Park DS, Kang HW, Kim JG, et al. (2005) The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice. Nucleic Acids Res 33: 577-586.
    • (2005) Nucleic Acids Res , vol.33 , pp. 577-586
    • Lee, B.M.1    Park, Y.J.2    Park, D.S.3    Kang, H.W.4    Kim, J.G.5
  • 24
    • 30944445669 scopus 로고    scopus 로고
    • Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity
    • Ochiai H, Inoue V, Takeya M, Sasaki A, Kaku H, (2005) Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity. Jpn Agric Res Q 39: 275-287.
    • (2005) Jpn Agric Res Q , vol.39 , pp. 275-287
    • Ochiai, H.1    Inoue, V.2    Takeya, M.3    Sasaki, A.4    Kaku, H.5
  • 25
    • 46049099151 scopus 로고    scopus 로고
    • Genome sequence and rapid evolution of the rice pathogen Xanthomonas oryzae pv. oryzae PXO99A
    • Salzberg SL, Sommer DD, Schatz MC, Phillippy AM, Rabinowicz PD, et al. (2008) Genome sequence and rapid evolution of the rice pathogen Xanthomonas oryzae pv. oryzae PXO99A. BMC Genomics 9: 204.
    • (2008) BMC Genomics , vol.9 , pp. 204
    • Salzberg, S.L.1    Sommer, D.D.2    Schatz, M.C.3    Phillippy, A.M.4    Rabinowicz, P.D.5
  • 26
    • 77950660340 scopus 로고    scopus 로고
    • Novel insights into the genomic basis of citrus canker based on the genome sequences of two strains of Xanthomonas fuscans subsp. aurantifolii
    • Moreira LM, Almeida NF Jr, Potnis N, Digiampietri LA, Adi SS, et al. (2010) Novel insights into the genomic basis of citrus canker based on the genome sequences of two strains of Xanthomonas fuscans subsp. aurantifolii. BMC Genomics 11: 238.
    • (2010) BMC Genomics , vol.11 , pp. 238
    • Moreira, L.M.1    Almeida Jr., N.F.2    Potnis, N.3    Digiampietri, L.A.4    Adi, S.S.5
  • 28
    • 0029941238 scopus 로고    scopus 로고
    • The Agrobacterium tumefaciens virB7 gene product, a proposed component of the T-complex transport apparatus, is a membrane-associated lipoprotein exposed at the periplasmic surface
    • Fernandez D, Dang TA, Spudich GM, Zhou XR, Berger BR, et al. (1996) The Agrobacterium tumefaciens virB7 gene product, a proposed component of the T-complex transport apparatus, is a membrane-associated lipoprotein exposed at the periplasmic surface. J Bacteriol 178: 3156-3167.
    • (1996) J Bacteriol , vol.178 , pp. 3156-3167
    • Fernandez, D.1    Dang, T.A.2    Spudich, G.M.3    Zhou, X.R.4    Berger, B.R.5
  • 29
    • 19344374255 scopus 로고    scopus 로고
    • The mating pair formation system of conjugative plasmids-A versatile secretion machinery for transfer of proteins and DNA
    • Schroder G, Lanka E, (2005) The mating pair formation system of conjugative plasmids-A versatile secretion machinery for transfer of proteins and DNA. Plasmid 54: 1-25.
    • (2005) Plasmid , vol.54 , pp. 1-25
    • Schroder, G.1    Lanka, E.2
  • 30
    • 0029795239 scopus 로고    scopus 로고
    • Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus
    • Spudich GM, Fernandez D, Zhou XR, Christie PJ, (1996) Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus. Proc Natl Acad Sci U S A 93: 7512-7517.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7512-7517
    • Spudich, G.M.1    Fernandez, D.2    Zhou, X.R.3    Christie, P.J.4
  • 31
    • 0030920071 scopus 로고    scopus 로고
    • Delineation of the interaction domains of Agrobacterium tumefaciens VirB7 and VirB9 by use of the yeast two-hybrid assay
    • Das A, Anderson LB, Xie YH, (1997) Delineation of the interaction domains of Agrobacterium tumefaciens VirB7 and VirB9 by use of the yeast two-hybrid assay. J Bacteriol 179: 3404-3409.
    • (1997) J Bacteriol , vol.179 , pp. 3404-3409
    • Das, A.1    Anderson, L.B.2    Xie, Y.H.3
  • 32
    • 0037143759 scopus 로고    scopus 로고
    • Peptide linkage mapping of the Agrobacterium tumefaciens vir-encoded type IV secretion system reveals protein subassemblies
    • Ward DV, Draper O, Zupan JR, Zambryski PC, (2002) Peptide linkage mapping of the Agrobacterium tumefaciens vir-encoded type IV secretion system reveals protein subassemblies. Proc Natl Acad Sci U S A 99: 11493-11500.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11493-11500
    • Ward, D.V.1    Draper, O.2    Zupan, J.R.3    Zambryski, P.C.4
  • 33
  • 34
    • 72949109740 scopus 로고    scopus 로고
    • Structure of the outer membrane complex of a type IV secretion system
    • Chandran V, Fronzes R, Duquerroy S, Cronin N, Navaza J, et al. (2009) Structure of the outer membrane complex of a type IV secretion system. Nature 462: 1011-1015.
    • (2009) Nature , vol.462 , pp. 1011-1015
    • Chandran, V.1    Fronzes, R.2    Duquerroy, S.3    Cronin, N.4    Navaza, J.5
  • 35
    • 33846794787 scopus 로고    scopus 로고
    • NMR structure of a complex between the VirB9/VirB7 interaction domains of the pKM101 type IV secretion system
    • Bayliss R, Harris R, Coutte L, Monier A, Fronzes R, et al. (2007) NMR structure of a complex between the VirB9/VirB7 interaction domains of the pKM101 type IV secretion system. Proc Natl Acad Sci U S A 104: 1673-1678.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1673-1678
    • Bayliss, R.1    Harris, R.2    Coutte, L.3    Monier, A.4    Fronzes, R.5
  • 36
    • 0035217633 scopus 로고    scopus 로고
    • Conjugal type IV macromolecular transfer systems of Gram-negative bacteria: organismal distribution, structural constraints and evolutionary conclusions
    • Cao TB, Saier MH Jr, (2001) Conjugal type IV macromolecular transfer systems of Gram-negative bacteria: organismal distribution, structural constraints and evolutionary conclusions. Microbiology 147: 3201-3214.
    • (2001) Microbiology , vol.147 , pp. 3201-3214
    • Cao, T.B.1    Saier Jr., M.H.2
  • 37
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Guntert P, Wuthrich K, (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319: 209-227.
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 38
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • Bax A, (2003) Weak alignment offers new NMR opportunities to study protein structure and dynamics. Protein Sci 12: 1-16.
    • (2003) Protein Sci , vol.12 , pp. 1-16
    • Bax, A.1
  • 39
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • Cornilescu G, Marquardt JL, Ottiger M, Bax A, (1998) Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J Am Chem Soc 120: 6836-6837.
    • (1998) J Am Chem Soc , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 40
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: a hawk-eyed view of biomolecular structure
    • Bax A, Grishaev A, (2005) Weak alignment NMR: a hawk-eyed view of biomolecular structure. Curr Opin Struct Biol 15: 563-570.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 41
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: a protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C, Boelens R, Bonvin AM, (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J Am Chem Soc 125: 1731-1737.
    • (2003) J Am Chem Soc , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 42
    • 0029891713 scopus 로고    scopus 로고
    • The Agrobacterium tumefaciens VirB7 lipoprotein is required for stabilization of VirB proteins during assembly of the T-complex transport apparatus
    • Fernandez D, Spudich GM, Zhou XR, Christie PJ, (1996) The Agrobacterium tumefaciens VirB7 lipoprotein is required for stabilization of VirB proteins during assembly of the T-complex transport apparatus. J Bacteriol 178: 3168-3176.
    • (1996) J Bacteriol , vol.178 , pp. 3168-3176
    • Fernandez, D.1    Spudich, G.M.2    Zhou, X.R.3    Christie, P.J.4
  • 43
    • 42049098107 scopus 로고    scopus 로고
    • Comparative and functional genomics reveals genetic diversity and determinants of host specificity among reference strains and a large collection of Chinese isolates of the phytopathogen Xanthomonas campestris pv. campestris
    • He YQ, Zhang L, Jiang BL, Zhang ZC, Xu RQ, et al. (2007) Comparative and functional genomics reveals genetic diversity and determinants of host specificity among reference strains and a large collection of Chinese isolates of the phytopathogen Xanthomonas campestris pv. campestris. Genome Biol 8: R218.
    • (2007) Genome Biol , vol.8
    • He, Y.Q.1    Zhang, L.2    Jiang, B.L.3    Zhang, Z.C.4    Xu, R.Q.5
  • 44
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L, Sander C, (1996) Mapping the protein universe. Science 273: 595-603.
    • (1996) Science , vol.273 , pp. 595-603
    • Holm, L.1    Sander, C.2
  • 46
    • 28244476414 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli
    • Garcia-Herrero A, Vogel HJ, (2005) Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli. Mol Microbiol 58: 1226-1237.
    • (2005) Mol Microbiol , vol.58 , pp. 1226-1237
    • Garcia-Herrero, A.1    Vogel, H.J.2
  • 47
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov KV, Pardon E, Steyaert J, Hol WG, (2009) Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 17: 255-265.
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 48
    • 66149092022 scopus 로고    scopus 로고
    • A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system
    • Spreter T, Yip CK, Sanowar S, Andre I, Kimbrough TG, et al. (2009) A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system. Nat Struct Mol Biol 16: 468-476.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 468-476
    • Spreter, T.1    Yip, C.K.2    Sanowar, S.3    Andre, I.4    Kimbrough, T.G.5
  • 50
    • 24644442568 scopus 로고    scopus 로고
    • Structure of the central hub of bacteriophage Mu baseplate determined by X-ray crystallography of gp44
    • Kondou Y, Kitazawa D, Takeda S, Tsuchiya Y, Yamashita E, et al. (2005) Structure of the central hub of bacteriophage Mu baseplate determined by X-ray crystallography of gp44. J Mol Biol 352: 976-985.
    • (2005) J Mol Biol , vol.352 , pp. 976-985
    • Kondou, Y.1    Kitazawa, D.2    Takeda, S.3    Tsuchiya, Y.4    Yamashita, E.5
  • 51
    • 61849164427 scopus 로고    scopus 로고
    • Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin
    • Leiman PG, Basler M, Ramagopal UA, Bonanno JB, Sauder JM, et al. (2009) Type VI secretion apparatus and phage tail-associated protein complexes share a common evolutionary origin. Proc Natl Acad Sci U S A 106: 4154-4159.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4154-4159
    • Leiman, P.G.1    Basler, M.2    Ramagopal, U.A.3    Bonanno, J.B.4    Sauder, J.M.5
  • 52
    • 77950243326 scopus 로고    scopus 로고
    • Identification of the gate regions in the primary structure of the secretin pIV
    • Spagnuolo J, Opalka N, Wen WX, Gagic D, Chabaud E, et al. (2010) Identification of the gate regions in the primary structure of the secretin pIV. Mol Microbiol 76: 133-150.
    • (2010) Mol Microbiol , vol.76 , pp. 133-150
    • Spagnuolo, J.1    Opalka, N.2    Wen, W.X.3    Gagic, D.4    Chabaud, E.5
  • 53
    • 78449265558 scopus 로고    scopus 로고
    • Crystal Structure of Legionella DotD: Insights into the Relationship between Type IVB and Type II/III Secretion Systems
    • Nakano N, Kubori T, Kinoshita M, Imada K, Nagai H, (2010) Crystal Structure of Legionella DotD: Insights into the Relationship between Type IVB and Type II/III Secretion Systems. PLoS Pathog 6: e1001129.
    • (2010) PLoS Pathog , vol.6
    • Nakano, N.1    Kubori, T.2    Kinoshita, M.3    Imada, K.4    Nagai, H.5
  • 54
    • 0034255091 scopus 로고    scopus 로고
    • Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells
    • Christie PJ, Vogel JP, (2000) Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells. Trends Microbiol 8: 354-360.
    • (2000) Trends Microbiol , vol.8 , pp. 354-360
    • Christie, P.J.1    Vogel, J.P.2
  • 55
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M, Schleucher J, Griesinger C, (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog NMR Spectrosc 34: 93-158.
    • (1999) Prog NMR Spectrosc , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 56
    • 0030018695 scopus 로고    scopus 로고
    • Magnetic field dependence of nitrogen-proton J splittings in N-15-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling
    • Tjandra N, Grzesiek S, Bax A, (1996) Magnetic field dependence of nitrogen-proton J splittings in N-15-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling. J Am Chem Soc 118: 6264-6272.
    • (1996) J Am Chem Soc , vol.118 , pp. 6264-6272
    • Tjandra, N.1    Grzesiek, S.2    Bax, A.3
  • 57
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • Ruckert M, Otting G, (2000) Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments. J Am Chem Soc 122: 7793-7797.
    • (2000) J Am Chem Soc , vol.122 , pp. 7793-7797
    • Ruckert, M.1    Otting, G.2
  • 58
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR
    • Zweckstetter M, Bax A, (2000) Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR. J Am Chem Soc 122: 3791-3792.
    • (2000) J Am Chem Soc , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 59
    • 0034884233 scopus 로고    scopus 로고
    • A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings
    • Dosset P, Hus JC, Marion D, Blackledge M, (2001) A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings. J Biomol NMR 20: 223-231.
    • (2001) J Biomol NMR , vol.20 , pp. 223-231
    • Dosset, P.1    Hus, J.C.2    Marion, D.3    Blackledge, M.4
  • 60
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 61
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: development of a software pipeline
    • Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, et al. (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59: 687-696.
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Stevens, T.J.3    Fogh, R.H.4    Pajon, A.5
  • 62
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G, Delaglio F, Bax A, (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13: 289-302.
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 63
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM, (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477-486.
    • (1996) J Biomol NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 64
    • 33847079676 scopus 로고    scopus 로고
    • Evaluating protein structures determined by structural genomics consortia
    • Bhattacharya A, Tejero R, Montelione GT, (2007) Evaluating protein structures determined by structural genomics consortia. Proteins 66: 778-795.
    • (2007) Proteins , vol.66 , pp. 778-795
    • Bhattacharya, A.1    Tejero, R.2    Montelione, G.T.3
  • 65
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K, (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55, 29-32.
    • (1996) J Mol Graph , vol.14
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 66
    • 0034048847 scopus 로고    scopus 로고
    • Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data
    • Dosset P, Hus JC, Blackledge M, Marion D, (2000) Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. J Biomol NMR 16: 23-28.
    • (2000) J Biomol NMR , vol.16 , pp. 23-28
    • Dosset, P.1    Hus, J.C.2    Blackledge, M.3    Marion, D.4
  • 67
    • 0028282555 scopus 로고
    • Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation
    • Farrow NA, Muhandiram R, Singer AU, Pascal SM, Kay CM, et al. (1994) Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. Biochemistry 33: 5984-6003.
    • (1994) Biochemistry , vol.33 , pp. 5984-6003
    • Farrow, N.A.1    Muhandiram, R.2    Singer, A.U.3    Pascal, S.M.4    Kay, C.M.5
  • 69
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins
    • Mulder FA, Schipper D, Bott R, Boelens R, (1999) Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins. J Mol Biol 292: 111-123.
    • (1999) J Mol Biol , vol.292 , pp. 111-123
    • Mulder, F.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4
  • 70
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J, (1996) Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 118: 11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 71
    • 0032968133 scopus 로고    scopus 로고
    • Implicit solvent models
    • Roux B, Simonson T, (1999) Implicit solvent models. Biophys Chem 78: 1-20.
    • (1999) Biophys Chem , vol.78 , pp. 1-20
    • Roux, B.1    Simonson, T.2
  • 72
    • 46249092554 scopus 로고    scopus 로고
    • Gromacs 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E, (2008) Gromacs 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 73
    • 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
  • 75
    • 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 Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 77
    • 0028103275 scopus 로고
    • The CCP4 Suite - Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 (1994) The CCP4 Suite- Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 78
    • 0000243829 scopus 로고
    • Procheck - a program to check the stereochemical quality of protein structures
    • Laskowski RA, Macarthur MW, Moss DS, Thornton JM, (1993) Procheck- a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26: 283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 80
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5
  • 81
    • 58149316599 scopus 로고    scopus 로고
    • Deciphering the role of the electrostatic interactions in the alpha-tropomyosin head-to-tail complex
    • Correa F, Salinas RK, Bonvin AM, Farah CS, (2008) Deciphering the role of the electrostatic interactions in the alpha-tropomyosin head-to-tail complex. Proteins 73: 902-917.
    • (2008) Proteins , vol.73 , pp. 902-917
    • Correa, F.1    Salinas, R.K.2    Bonvin, A.M.3    Farah, C.S.4
  • 82
    • 34047239634 scopus 로고    scopus 로고
    • Different effects of trifluoroethanol and glycerol on the stability of tropomyosin helices and the head-to-tail complex
    • Correa F, Farah CS, (2007) Different effects of trifluoroethanol and glycerol on the stability of tropomyosin helices and the head-to-tail complex. Biophys J 92: 2463-2475.
    • (2007) Biophys J , vol.92 , pp. 2463-2475
    • Correa, F.1    Farah, C.S.2
  • 83
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schagger H, (2006) Tricine-SDS-PAGE. Nat Protoc 1: 16-22.
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schagger, H.1
  • 84
    • 70349968208 scopus 로고    scopus 로고
    • PILZ protein structure and interactions with PILB and the FIMX EAL domain: implications for control of type IV pilus biogenesis
    • Guzzo CR, Salinas RK, Andrade MO, Farah CS, (2009) PILZ protein structure and interactions with PILB and the FIMX EAL domain: implications for control of type IV pilus biogenesis. J Mol Biol 393: 848-866.
    • (2009) J Mol Biol , vol.393 , pp. 848-866
    • Guzzo, C.R.1    Salinas, R.K.2    Andrade, M.O.3    Farah, C.S.4
  • 85
    • 0027570304 scopus 로고
    • Gene-for-genes interactions between cotton R genes and Xanthomonas campestris pv. malvacearum avr genes
    • De Feyter R, Yang Y, Gabriel DW, (1993) Gene-for-genes interactions between cotton R genes and Xanthomonas campestris pv. malvacearum avr genes. Mol Plant Microbe Interact 6: 225-237.
    • (1993) Mol Plant Microbe Interact , vol.6 , pp. 225-237
    • de Feyter, R.1    Yang, Y.2    Gabriel, D.W.3
  • 86
    • 0030043747 scopus 로고    scopus 로고
    • Expression and localization of HrpA1, a protein of Xanthomonas campestris pv. vesicatoria essential for pathogenicity and induction of the hypersensitive reaction
    • Wengelnik K, Marie C, Russel M, Bonas U, (1996) Expression and localization of HrpA1, a protein of Xanthomonas campestris pv. vesicatoria essential for pathogenicity and induction of the hypersensitive reaction. J Bacteriol 178: 1061-1069.
    • (1996) J Bacteriol , vol.178 , pp. 1061-1069
    • Wengelnik, K.1    Marie, C.2    Russel, M.3    Bonas, U.4
  • 87
    • 10344225117 scopus 로고    scopus 로고
    • Agrobacterium VirB10, an ATP energy sensor required for type IV secretion
    • Cascales E, Christie PJ, (2004) Agrobacterium VirB10, an ATP energy sensor required for type IV secretion. Proc Natl Acad Sci U S A 101: 17228-17233.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17228-17233
    • Cascales, E.1    Christie, P.J.2
  • 88
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 89
    • 1442306656 scopus 로고    scopus 로고
    • Assignment validation software suite for the evaluation and presentation of protein resonance assignment data
    • Moseley HN, Sahota G, Montelione GT, (2004) Assignment validation software suite for the evaluation and presentation of protein resonance assignment data. J Biomol NMR 28: 341-355.
    • (2004) J Biomol NMR , vol.28 , pp. 341-355
    • Moseley, H.N.1    Sahota, G.2    Montelione, G.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.