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Volumn 83, Issue 2, 2012, Pages 275-288

The conjugation protein TcpC from Clostridium perfringens is structurally related to the type IV secretion system protein VirB8 from Gram-negative bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; NTF2 LIKE DOMAIN PROTEIN; PROTEIN TCPA; PROTEIN TCPC; PROTEIN TCPG; PROTEIN TCPH; PROTEIN VIRB8; TETRACYCLINE; UNCLASSIFIED DRUG;

EID: 84855804851     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2011.07930.x     Document Type: Article
Times cited : (66)

References (68)
  • 1
    • 33947121550 scopus 로고    scopus 로고
    • A type IV-secretion-like system is required for conjugative DNA transport of broad-host-range plasmid pIP501 in gram-positive bacteria
    • Abajy, M. Y., Kopec, J., Schiwon, K., Burzynski, M., Doring, M., Bohn, C., and Grohmann, E. (2007) A type IV-secretion-like system is required for conjugative DNA transport of broad-host-range plasmid pIP501 in gram-positive bacteria. J Bacteriol 189: 2487-2496.
    • (2007) J Bacteriol , vol.189 , pp. 2487-2496
    • Abajy, M.Y.1    Kopec, J.2    Schiwon, K.3    Burzynski, M.4    Doring, M.5    Bohn, C.6    Grohmann, E.7
  • 3
    • 71449116162 scopus 로고    scopus 로고
    • Biological diversity of prokaryotic type IV secretion systems
    • Alvarez-Martinez, C.E., and Christie, P.J. (2009) Biological diversity of prokaryotic type IV secretion systems. Microbiol Mol Biol Rev 73: 775-808.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 775-808
    • Alvarez-Martinez, C.E.1    Christie, P.J.2
  • 4
    • 0036174712 scopus 로고    scopus 로고
    • Continuum secondary structure captures protein flexibility
    • Andersen, C.A., Palmer, A.G., Brunak, S., and Rost, B. (2002) Continuum secondary structure captures protein flexibility. Structure 10: 175-184.
    • (2002) Structure , vol.10 , pp. 175-184
    • Andersen, C.A.1    Palmer, A.G.2    Brunak, S.3    Rost, B.4
  • 6
    • 33644524053 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens VirB8 structure reveals potential protein-protein interaction sites
    • Bailey, S., Ward, D., Middleton, R., Grossmann, J.G., and Zambryski, P.C. (2006) Agrobacterium tumefaciens VirB8 structure reveals potential protein-protein interaction sites. Proc Natl Acad Sci USA 103: 2582-2587.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2582-2587
    • Bailey, S.1    Ward, D.2    Middleton, R.3    Grossmann, J.G.4    Zambryski, P.C.5
  • 7
    • 0027263622 scopus 로고
    • Clostridium perfringens-Escherichia coli shuttle vectors that carry single antibiotic resistance determinants
    • Bannam, T.L., and Rood, J.I. (1993) Clostridium perfringens-Escherichia coli shuttle vectors that carry single antibiotic resistance determinants. Plasmid 29: 233-235.
    • (1993) Plasmid , vol.29 , pp. 233-235
    • Bannam, T.L.1    Rood, J.I.2
  • 8
    • 33745440551 scopus 로고    scopus 로고
    • Functional identification of conjugation and replication regions of the tetracycline resistance plasmid pCW3 from Clostridium perfringens
    • Bannam, T.L., Teng, W.L., Bulach, D., Lyras, D., and Rood, J.I. (2006) Functional identification of conjugation and replication regions of the tetracycline resistance plasmid pCW3 from Clostridium perfringens. J Bacteriol 188: 4942-4951.
    • (2006) J Bacteriol , vol.188 , pp. 4942-4951
    • Bannam, T.L.1    Teng, W.L.2    Bulach, D.3    Lyras, D.4    Rood, J.I.5
  • 9
    • 33947431670 scopus 로고    scopus 로고
    • VirB8: a conserved type IV secretion system assembly factor and drug target
    • Baron, C. (2006) VirB8: a conserved type IV secretion system assembly factor and drug target. Biochem Cell Biol 84: 890-899.
    • (2006) Biochem Cell Biol , vol.84 , pp. 890-899
    • Baron, C.1
  • 10
    • 0030593377 scopus 로고    scopus 로고
    • The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2)
    • Bullock, T.L., Clarkson, W.D., Kent, H.M., and Stewart, M. (1996) The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2). J Mol Biol 260: 422-431.
    • (1996) J Mol Biol , vol.260 , pp. 422-431
    • Bullock, T.L.1    Clarkson, W.D.2    Kent, H.M.3    Stewart, M.4
  • 11
    • 33745258636 scopus 로고    scopus 로고
    • Investigating the basis of substrate recognition in the pC221 relaxosome
    • Caryl, J.A., and Thomas, C.D. (2006) Investigating the basis of substrate recognition in the pC221 relaxosome. Mol Microbiol 60: 1302-1318.
    • (2006) Mol Microbiol , vol.60 , pp. 1302-1318
    • Caryl, J.A.1    Thomas, C.D.2
  • 12
    • 1842456892 scopus 로고    scopus 로고
    • The versatile bacterial type IV secretion systems
    • Cascales, E., and Christie, P.J. (2003) The versatile bacterial type IV secretion systems. Nat Rev Microbiol 1: 137-149.
    • (2003) Nat Rev Microbiol , vol.1 , pp. 137-149
    • Cascales, E.1    Christie, P.J.2
  • 13
    • 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., and Waksman, G. (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    Waksman, G.6
  • 15
    • 33847005432 scopus 로고    scopus 로고
    • Specificity determinants of conjugative DNA processing in the Enterococcus faecalis plasmid pCF10 and the Lactococcus lactis plasmid pRS01
    • Chen, Y., Staddon, J.H., and Dunny, G.M. (2007) Specificity determinants of conjugative DNA processing in the Enterococcus faecalis plasmid pCF10 and the Lactococcus lactis plasmid pRS01. Mol Microbiol 63: 1549-1564.
    • (2007) Mol Microbiol , vol.63 , pp. 1549-1564
    • Chen, Y.1    Staddon, J.H.2    Dunny, G.M.3
  • 16
    • 72949115254 scopus 로고    scopus 로고
    • Structural biology: translocation chamber's secrets
    • Christie, P.J. (2009) Structural biology: translocation chamber's secrets. Nature 462: 992-994.
    • (2009) Nature , vol.462 , pp. 992-994
    • Christie, P.J.1
  • 17
    • 0036355267 scopus 로고    scopus 로고
    • Fully automated screening systems
    • Cohen, S., and Trinka, R.F. (2002) Fully automated screening systems. Methods Mol Biol 190: 213-228.
    • (2002) Methods Mol Biol , vol.190 , pp. 213-228
    • Cohen, S.1    Trinka, R.F.2
  • 18
    • 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
  • 19
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley, P., and 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
  • 20
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans, P. (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62: 72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 23
    • 0037905748 scopus 로고    scopus 로고
    • Conjugative plasmid transfer in gram-positive bacteria
    • Grohmann, E., Muth, G., and Espinosa, M. (2003) Conjugative plasmid transfer in gram-positive bacteria. Microbiol Mol Biol Rev 67: 277-301.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 277-301
    • Grohmann, E.1    Muth, G.2    Espinosa, M.3
  • 24
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 25
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm, L., Kaariainen, S., Rosenstrom, P., and Schenkel, A. (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24: 2780-2781.
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 26
    • 27744568778 scopus 로고    scopus 로고
    • The putative lytic transglycosylase VirB1 from Brucella suis interacts with the type IV secretion system core components VirB8, VirB9 and VirB11
    • Hoppner, C., Carle, A., Sivanesan, D., Hoeppner, S., and Baron, C. (2005) The putative lytic transglycosylase VirB1 from Brucella suis interacts with the type IV secretion system core components VirB8, VirB9 and VirB11. Microbiology 151: 3469-3482.
    • (2005) Microbiology , vol.151 , pp. 3469-3482
    • Hoppner, C.1    Carle, A.2    Sivanesan, D.3    Hoeppner, S.4    Baron, C.5
  • 27
    • 0037195792 scopus 로고    scopus 로고
    • Purification and properties of TrwB, a hexameric, ATP-binding integral membrane protein essential for R388 plasmid conjugation
    • Hormaeche, I., Alkorta, I., Moro, F., Valpuesta, J.M., Goni, F.M., and De La Cruz, F. (2002) Purification and properties of TrwB, a hexameric, ATP-binding integral membrane protein essential for R388 plasmid conjugation. J Biol Chem 277: 46456-46462.
    • (2002) J Biol Chem , vol.277 , pp. 46456-46462
    • Hormaeche, I.1    Alkorta, I.2    Moro, F.3    Valpuesta, J.M.4    Goni, F.M.5    De La Cruz, F.6
  • 29
    • 0033749654 scopus 로고    scopus 로고
    • A bacterial two-hybrid system that exploits a cAMP signaling cascade in Escherichia coli
    • Karimova, G., Ullmann, A., and Ladant, D. (2000) A bacterial two-hybrid system that exploits a cAMP signaling cascade in Escherichia coli. Methods Enzymol 328: 59-73.
    • (2000) Methods Enzymol , vol.328 , pp. 59-73
    • Karimova, G.1    Ullmann, A.2    Ladant, D.3
  • 30
    • 15244361175 scopus 로고    scopus 로고
    • Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis
    • Karimova, G., Dautin, N., and Ladant, D. (2005) Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis. J Bacteriol 187: 2233-2243.
    • (2005) J Bacteriol , vol.187 , pp. 2233-2243
    • Karimova, G.1    Dautin, N.2    Ladant, D.3
  • 32
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 33
    • 0034059337 scopus 로고    scopus 로고
    • Subcellular localization of the Agrobacterium tumefaciens T-DNA transport pore proteins: VirB8 is essential for the assembly of the transport pore
    • Kumar, R.B., Xie, Y.H., and Das, A. (2000) Subcellular localization of the Agrobacterium tumefaciens T-DNA transport pore proteins: VirB8 is essential for the assembly of the transport pore. Mol Microbiol 36: 608-617.
    • (2000) Mol Microbiol , vol.36 , pp. 608-617
    • Kumar, R.B.1    Xie, Y.H.2    Das, A.3
  • 34
    • 33645098517 scopus 로고    scopus 로고
    • The TraA relaxase autoregulates the putative type IV secretion-like system encoded by the broad-host-range Streptococcus agalactiae plasmid pIP501
    • Kurenbach, B., Kopec, J., Magdefrau, M., Andreas, K., Keller, W., Bohn, C., etal. (2006) The TraA relaxase autoregulates the putative type IV secretion-like system encoded by the broad-host-range Streptococcus agalactiae plasmid pIP501. Microbiology 152: 637-645.
    • (2006) Microbiology , vol.152 , pp. 637-645
    • Kurenbach, B.1    Kopec, J.2    Magdefrau, M.3    Andreas, K.4    Keller, W.5    Bohn, C.6
  • 35
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S.X., Lamzin, V.S., and Perrakis, A. (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat Protoc 3: 1171-1179.
    • (2008) Nat Protoc , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 36
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence, M.C., and Colman, P.M. (1993) Shape complementarity at protein/protein interfaces. J Mol Biol 234: 946-950.
    • (1993) J Mol Biol , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 38
    • 0036047412 scopus 로고    scopus 로고
    • Bacterial conjugation: a two-step mechanism for DNA transport
    • Llosa, M., Gomis-Ruth, F.X., Coll, M., and de la Cruz, F. (2002) Bacterial conjugation: a two-step mechanism for DNA transport. Mol Microbiol 45: 1-8.
    • (2002) Mol Microbiol , vol.45 , pp. 1-8
    • Llosa, M.1    Gomis-Ruth, F.X.2    Coll, M.3    de la Cruz, F.4
  • 39
    • 1642483709 scopus 로고    scopus 로고
    • The large resolvase TnpX is the only transposon-encoded protein required for transposition of the Tn4451/3 family of integrative mobilizable elements
    • Lyras, D., Adams, V., Lucet, I., and Rood, J.I. (2004) The large resolvase TnpX is the only transposon-encoded protein required for transposition of the Tn4451/3 family of integrative mobilizable elements. Mol Microbiol 51: 1787-1800.
    • (2004) Mol Microbiol , vol.51 , pp. 1787-1800
    • Lyras, D.1    Adams, V.2    Lucet, I.3    Rood, J.I.4
  • 40
    • 0036849859 scopus 로고    scopus 로고
    • Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines
    • McPhillips, T.M., McPhillips, S.E., Chiu, H.J., Cohen, A.E., Deacon, A.M., Ellis, P.J., etal. (2002) Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines. J Synchrotron Radiat 9: 401-406.
    • (2002) J Synchrotron Radiat , vol.9 , pp. 401-406
    • McPhillips, T.M.1    McPhillips, S.E.2    Chiu, H.J.3    Cohen, A.E.4    Deacon, A.M.5    Ellis, P.J.6
  • 41
  • 42
  • 43
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter, J., and Merrit, E.A. (2006) TLSMD web server for the generation of multi-group TLS models. J Appl Crystallogr 39: 109-111.
    • (2006) J Appl Crystallogr , vol.39 , pp. 109-111
    • Painter, J.1    Merrit, E.A.2
  • 44
    • 35648948908 scopus 로고    scopus 로고
    • TcpA, an FtsK/SpoIIIE homolog, is essential for transfer of the conjugative plasmid pCW3 in Clostridium perfringens
    • Parsons, J.A., Bannam, T.L., Devenish, R.J., and Rood, J.I. (2007) TcpA, an FtsK/SpoIIIE homolog, is essential for transfer of the conjugative plasmid pCW3 in Clostridium perfringens. J Bacteriol 189: 7782-7790.
    • (2007) J Bacteriol , vol.189 , pp. 7782-7790
    • Parsons, J.A.1    Bannam, T.L.2    Devenish, R.J.3    Rood, J.I.4
  • 45
    • 33646598357 scopus 로고    scopus 로고
    • Dimerization and interactions of Brucella suis VirB8 with VirB4 and VirB10 are required for its biological activity
    • Paschos, A., Patey, G., Sivanesan, D., Gao, C., Bayliss, R., Waksman, G., etal. (2006) Dimerization and interactions of Brucella suis VirB8 with VirB4 and VirB10 are required for its biological activity. Proc Natl Acad Sci USA 103: 7252-7257.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7252-7257
    • Paschos, A.1    Patey, G.2    Sivanesan, D.3    Gao, C.4    Bayliss, R.5    Waksman, G.6
  • 46
    • 0029320145 scopus 로고
    • A versatile quick-prep of genomic DNA from gram-positive bacteria
    • Pospiech, A., and Neumann, B. (1995) A versatile quick-prep of genomic DNA from gram-positive bacteria. Trends Genet 11: 217-218.
    • (1995) Trends Genet , vol.11 , pp. 217-218
    • Pospiech, A.1    Neumann, B.2
  • 48
    • 0036094278 scopus 로고    scopus 로고
    • The PtlE protein of Bordetella pertussis has peptidoglycanase activity required for Ptl-mediated pertussis toxin secretion
    • Rambow-Larsen, A.A., and Weiss, A.A. (2002) The PtlE protein of Bordetella pertussis has peptidoglycanase activity required for Ptl-mediated pertussis toxin secretion. J Bacteriol 184: 2863-2869.
    • (2002) J Bacteriol , vol.184 , pp. 2863-2869
    • Rambow-Larsen, A.A.1    Weiss, A.A.2
  • 49
    • 0021017779 scopus 로고
    • Transferable tetracycline resistance in Clostridium perfringens strains of porcine origin
    • Rood, J.I. (1983) Transferable tetracycline resistance in Clostridium perfringens strains of porcine origin. Can J Microbiol 29: 1241-1246.
    • (1983) Can J Microbiol , vol.29 , pp. 1241-1246
    • Rood, J.I.1
  • 50
    • 0018120429 scopus 로고
    • Identification of a transferable tetracycline resistance plasmid (pCW3) from Clostridium perfringens
    • Rood, J.I., Scott, V.N., and Duncan, C.L. (1978) Identification of a transferable tetracycline resistance plasmid (pCW3) from Clostridium perfringens. Plasmid 1: 563-570.
    • (1978) Plasmid , vol.1 , pp. 563-570
    • Rood, J.I.1    Scott, V.N.2    Duncan, C.L.3
  • 51
    • 84855811829 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System. Schrödinger, LLC.
    • Schrödinger, L. (2008) The PyMOL Molecular Graphics System. Schrödinger, LLC.
    • (2008)
    • Schrödinger, L.1
  • 52
    • 0034668130 scopus 로고    scopus 로고
    • Determination of the sedimentation coefficient distribution by least-squares boundary modeling
    • Schuck, P., and Rossmanith, P. (2000) Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers 54: 328-341.
    • (2000) Biopolymers , vol.54 , pp. 328-341
    • Schuck, P.1    Rossmanith, P.2
  • 53
    • 0024436683 scopus 로고
    • Electroporation-mediated transformation of lysostaphin-treated Clostridium perfringens
    • Scott, P.T., and Rood, J.I. (1989) Electroporation-mediated transformation of lysostaphin-treated Clostridium perfringens. Gene 82: 327-333.
    • (1989) Gene , vol.82 , pp. 327-333
    • Scott, P.T.1    Rood, J.I.2
  • 54
    • 79955527260 scopus 로고    scopus 로고
    • The dimer interface of Agrobacterium tumefaciens VirB8 is important for type IV secretion system function, stability, and association of VirB2 with the core complex
    • Sivanesan, D., and Baron, C. (2011) The dimer interface of Agrobacterium tumefaciens VirB8 is important for type IV secretion system function, stability, and association of VirB2 with the core complex. J Bacteriol 193: 2097-2106.
    • (2011) J Bacteriol , vol.193 , pp. 2097-2106
    • Sivanesan, D.1    Baron, C.2
  • 55
    • 77952829868 scopus 로고    scopus 로고
    • Quantitative analysis of VirB8-VirB9-VirB10 interactions provides a dynamic model of type IV secretion system core complex assembly
    • Sivanesan, D., Hancock, M.A., Villamil Giraldo, A.M., and Baron, C. (2010) Quantitative analysis of VirB8-VirB9-VirB10 interactions provides a dynamic model of type IV secretion system core complex assembly. Biochemistry 49: 4483-4493.
    • (2010) Biochemistry , vol.49 , pp. 4483-4493
    • Sivanesan, D.1    Hancock, M.A.2    Villamil Giraldo, A.M.3    Baron, C.4
  • 56
    • 65549118438 scopus 로고    scopus 로고
    • The putative coupling protein TcpA interacts with other pCW3-encoded proteins to form an essential part of the conjugation complex
    • Steen, J.A., Bannam, T.L., Teng, W.L., Devenish, R.J., and Rood, J.I. (2009) The putative coupling protein TcpA interacts with other pCW3-encoded proteins to form an essential part of the conjugation complex. J Bacteriol 191: 2926-2933.
    • (2009) J Bacteriol , vol.191 , pp. 2926-2933
    • Steen, J.A.1    Bannam, T.L.2    Teng, W.L.3    Devenish, R.J.4    Rood, J.I.5
  • 58
    • 79953702794 scopus 로고    scopus 로고
    • Role of the cag-pathogenicity island encoded type IV secretion system in Helicobacter pylori pathogenesis
    • Tegtmeyer, N., Wessler, S., and Backert, S. (2011) Role of the cag-pathogenicity island encoded type IV secretion system in Helicobacter pylori pathogenesis. FEBS J 278: 1190-1202.
    • (2011) FEBS J , vol.278 , pp. 1190-1202
    • Tegtmeyer, N.1    Wessler, S.2    Backert, S.3
  • 59
    • 47249092882 scopus 로고    scopus 로고
    • Functional characterization and localization of the TcpH conjugation protein from Clostridium perfringens
    • Teng, W.L., Bannam, T.L., Parsons, J.A., and Rood, J.I. (2008) Functional characterization and localization of the TcpH conjugation protein from Clostridium perfringens. J Bacteriol 190: 5075-5086.
    • (2008) J Bacteriol , vol.190 , pp. 5075-5086
    • Teng, W.L.1    Bannam, T.L.2    Parsons, J.A.3    Rood, J.I.4
  • 60
    • 15444380769 scopus 로고    scopus 로고
    • Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori
    • Terradot, L., Bayliss, R., Oomen, C., Leonard, G.A., Baron, C., and Waksman, G. (2005) Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori. Proc Natl Acad Sci USA 102: 4596-4601.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4596-4601
    • Terradot, L.1    Bayliss, R.2    Oomen, C.3    Leonard, G.A.4    Baron, C.5    Waksman, G.6
  • 62
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger, T.C. (2003) Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr D Biol Crystallogr 59: 38-44.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 65
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L., and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J Mol Biol 229: 105-124.
    • (1993) J Mol Biol , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 66
    • 77957116092 scopus 로고    scopus 로고
    • Type IV secretion systems: versatility and diversity in function
    • Wallden, K., Rivera-Calzada, A., and Waksman, G. (2010) Type IV secretion systems: versatility and diversity in function. Cell Microbiol 12: 1203-1212.
    • (2010) Cell Microbiol , vol.12 , pp. 1203-1212
    • Wallden, K.1    Rivera-Calzada, A.2    Waksman, G.3
  • 67
    • 0037143759 scopus 로고    scopus 로고
    • Peptide linkage mapping of the Agrobacterium tumefaciens vir-encoded type IV secretion system reveals protein subassemblies
    • Ward, D.V., Draper, O., Zupan, J.R., and Zambryski, P.C. (2002) Peptide linkage mapping of the Agrobacterium tumefaciens vir-encoded type IV secretion system reveals protein subassemblies. Proc Natl Acad Sci USA 99: 11493-11500.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11493-11500
    • Ward, D.V.1    Draper, O.2    Zupan, J.R.3    Zambryski, P.C.4
  • 68
    • 50449110851 scopus 로고    scopus 로고
    • Exposing plasmids as the Achilles' heel of drug-resistant bacteria
    • Williams, J.J., and Hergenrother, P.J. (2008) Exposing plasmids as the Achilles' heel of drug-resistant bacteria. Curr Opin Chem Biol 12: 389-399.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 389-399
    • Williams, J.J.1    Hergenrother, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.