메뉴 건너뛰기




Volumn 7, Issue 10, 1999, Pages 1301-1309

The structure of the outer membrane protein OmpX from Escherichia coil reveals possible mechanisms of virulence

Author keywords

Bacterial defense system; Coordination sphere; Integral membrane protein; OmpX; Platinum; X ray analysis; barrel

Indexed keywords

BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN;

EID: 0033570111     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)80063-5     Document Type: Article
Times cited : (264)

References (29)
  • 1
    • 0028027770 scopus 로고
    • Specificity of the complement resistance and cell association phenotypes encoded by the outer membrane protein genes rck from Salmonella typhimurium and ail from Yersinia enterocolitica
    • 1. Heffernan, E.J., Wu, L., Louie, J., Okamoto, S., Fierer, J. & Guiney, D.G. (1994). Specificity of the complement resistance and cell association phenotypes encoded by the outer membrane protein genes rck from Salmonella typhimurium and ail from Yersinia enterocolitica. Infect. Immun. 62, 5183-5186.
    • (1994) Infect. Immun. , vol.62 , pp. 5183-5186
    • Heffernan, E.J.1    Wu, L.2    Louie, J.3    Okamoto, S.4    Fierer, J.5    Guiney, D.G.6
  • 2
    • 0028900882 scopus 로고
    • Identification and characterization of an outer membrane protein, OmpX, in Escherichia coli that is homologous to a family of outer membrane proteins including Ail of Yersinia enterocolitica
    • 2. Mecsas, J., Welch, R., Erickson, J.W. & Gross, C.A. (1995). Identification and characterization of an outer membrane protein, OmpX, in Escherichia coli that is homologous to a family of outer membrane proteins including Ail of Yersinia enterocolitica. J. Bacteriol. 177, 799-804.
    • (1995) J. Bacteriol. , vol.177 , pp. 799-804
    • Mecsas, J.1    Welch, R.2    Erickson, J.W.3    Gross, C.A.4
  • 3
    • 0028089771 scopus 로고
    • Invasion of rabbit ileal tissue by Enterobacter cloacae varies with the concentration of OmpX in the outer membrane
    • 3. de Kort, G., Bolton, A., Martin, G., Stephen, J. & van de Klundert, J.A.M. (1994). Invasion of rabbit ileal tissue by Enterobacter cloacae varies with the concentration of OmpX in the outer membrane. Infect. Immun. 62, 4722-4726.
    • (1994) Infect. Immun. , vol.62 , pp. 4722-4726
    • De Kort, G.1    Bolton, A.2    Martin, G.3    Stephen, J.4    De Van Klundert, J.A.M.5
  • 4
    • 0023610908 scopus 로고
    • Cloning of a β-lactam resistance determinant of Enterobacter cloacae affecting outer membrane proteins of Enterobacteriaceae
    • 4. Stoorvogel, J., van Bussel, M.J.A.W.M. & van de Klundert, J.A.M. (1987). Cloning of a β-lactam resistance determinant of Enterobacter cloacae affecting outer membrane proteins of Enterobacteriaceae. FEMS Microbiol. Lett. 48, 277-281.
    • (1987) FEMS Microbiol. Lett. , vol.48 , pp. 277-281
    • Stoorvogel, J.1    Van Bussel, M.J.A.W.M.2    De Van Klundert, J.A.M.3
  • 5
    • 0031081284 scopus 로고    scopus 로고
    • Molecular characterization of a 17-kDa outer-membrane protein from Klebsiella pneumoniae
    • 5. Climent, N., Ferrer, S., Rubires, X., Merino, S., Tomás, J.M. & Regué, M. (1997). Molecular characterization of a 17-kDa outer-membrane protein from Klebsiella pneumoniae. Res. Microbiol. 148, 133-143.
    • (1997) Res. Microbiol. , vol.148 , pp. 133-143
    • Climent, N.1    Ferrer, S.2    Rubires, X.3    Merino, S.4    Tomás, J.M.5    Regué, M.6
  • 6
    • 0026051251 scopus 로고
    • A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein
    • 6. Pulkkinen, W.S. & Miller, S.I. (1991). A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein. J. Bacteriol. 173, 86-93.
    • (1991) J. Bacteriol. , vol.173 , pp. 86-93
    • Pulkkinen, W.S.1    Miller, S.I.2
  • 7
    • 0026687245 scopus 로고
    • Mechanism of resistance to complement-mediated killing of bacteria encoded by the Salmonella typhimurium virulence plasmid gene rck
    • 7. Heffernan, E.J., Reed, S., Hackett, J., Fierer, J., Roudier, C. & Guiney, D. (1992). Mechanism of resistance to complement-mediated killing of bacteria encoded by the Salmonella typhimurium virulence plasmid gene rck. J. Clin. Invest. 90, 953-964.
    • (1992) J. Clin. Invest. , vol.90 , pp. 953-964
    • Heffernan, E.J.1    Reed, S.2    Hackett, J.3    Fierer, J.4    Roudier, C.5    Guiney, D.6
  • 8
    • 0025008909 scopus 로고
    • Nucleotide sequence of the Yersinia enterocolitica ail gene and characterization of the Ail protein product
    • 8. Miller, V.L., Bliska, J.B. & Falkow, S. (1990). Nucleotide sequence of the Yersinia enterocolitica ail gene and characterization of the Ail protein product. J. Bacteriol. 172, 1062-1069.
    • (1990) J. Bacteriol. , vol.172 , pp. 1062-1069
    • Miller, V.L.1    Bliska, J.B.2    Falkow, S.3
  • 9
    • 0026568644 scopus 로고
    • Bacterial resistance to complement killing mediated by the Ail protein of Yersinia enterocolitica
    • 9. Bliska, J.B. & Falkow, S. (1992). Bacterial resistance to complement killing mediated by the Ail protein of Yersinia enterocolitica. Proc. Natl Acad. Sci. USA 89, 3561-3565.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3561-3565
    • Bliska, J.B.1    Falkow, S.2
  • 10
    • 0025079241 scopus 로고
    • A bacterial virulence determinant encoded by lysogenic coliphage λ
    • 10. Barondess, J.J. & Beckwith, J. (1990). A bacterial virulence determinant encoded by lysogenic coliphage λ. Nature 346, 871-874.
    • (1990) Nature , vol.346 , pp. 871-874
    • Barondess, J.J.1    Beckwith, J.2
  • 11
    • 0031278174 scopus 로고    scopus 로고
    • The lom gene of bacteriophage λ is involved in Escherichia coli K12 adhesion to human buccal epithelial cells
    • 11. Pacheco, S.V., González, O.G. & Contreras, G.L.P. (1997). The lom gene of bacteriophage λ is involved in Escherichia coli K12 adhesion to human buccal epithelial cells. FEMS Microbiol. Lett. 156, 129-132.
    • (1997) FEMS Microbiol. Lett. , vol.156 , pp. 129-132
    • Pacheco, S.V.1    González, O.G.2    Contreras, G.L.P.3
  • 12
    • 0033081475 scopus 로고    scopus 로고
    • Strategy for membrane protein crystallization exemplified with OmpA and OmpX
    • 12. Pautsch, A., Vogt, J., Model, K., Siebold, C. & Schulz, G.E. (1999). Strategy for membrane protein crystallization exemplified with OmpA and OmpX. Proteins 34, 167-172.
    • (1999) Proteins , vol.34 , pp. 167-172
    • Pautsch, A.1    Vogt, J.2    Model, K.3    Siebold, C.4    Schulz, G.E.5
  • 13
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • 13. Pautsch, A. & Schulz, G.E. (1998). Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol. 5, 1013-1017.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 14
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 14. Collaborative Computational Project Number 4 (1994). The CCP4 Suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 15
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • 15. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (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
  • 16
    • 0032579317 scopus 로고    scopus 로고
    • Shear numbers of protein β-barrels: Definition refinements and statistics
    • 16. Liu, W.-M. (1998). Shear numbers of protein β-barrels: definition refinements and statistics. J. Mol. Biol. 275, 541-545.
    • (1998) J. Mol. Biol. , vol.275 , pp. 541-545
    • Liu, W.-M.1
  • 17
    • 0026585553 scopus 로고
    • Amino acid substitutions in naturally occurring variants of Ail result in altered invasion activity
    • 17. Beer, K.B. & Miller, V.L. (1992). Amino acid substitutions in naturally occurring variants of Ail result in altered invasion activity. J. Bacteriol. 174, 1360-1369.
    • (1992) J. Bacteriol. , vol.174 , pp. 1360-1369
    • Beer, K.B.1    Miller, V.L.2
  • 18
    • 0029976558 scopus 로고    scopus 로고
    • Identification of a domain in rck, a product of the Salmonella typhimurium virulence plasmid, required for both serum resistance and cell invasion
    • 18. Cirillo, D.M., Heffernan, E.J., Wu, L., Harwood, J., Fierer, J. & Guiney, D.G. (1996). Identification of a domain in Rck, a product of the Salmonella typhimurium virulence plasmid, required for both serum resistance and cell invasion. Infect. Immun. 64, 2019-2023.
    • (1996) Infect. Immun. , vol.64 , pp. 2019-2023
    • Cirillo, D.M.1    Heffernan, E.J.2    Wu, L.3    Harwood, J.4    Fierer, J.5    Guiney, D.G.6
  • 19
    • 0031934123 scopus 로고    scopus 로고
    • Immuno-detection of the virulence determinant OmpX at the cell surface of Enterobacter cloacae
    • 19. de Kort, G., van der Bent-Klootwijk, P. & van de Klundert, J.A.M. (1998). Immuno-detection of the virulence determinant OmpX at the cell surface of Enterobacter cloacae. FEMS Microbiol. Lett. 158, 115-120.
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 115-120
    • De Kort, G.1    Van Der Bent-Klootwijk, P.2    De Van Klundert, J.A.M.3
  • 20
    • 0030220261 scopus 로고    scopus 로고
    • Porins: General to specific, native to engineered passive pores
    • 20. Schulz, G.E. (1996). Porins: general to specific, native to engineered passive pores. Curr. Opin. Struct. Biol. 6, 485-490.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 485-490
    • Schulz, G.E.1
  • 21
    • 0022517918 scopus 로고
    • Models of the structure of outer membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods
    • 21. Vogel, H. & Jähnig, F. (1986). Models of the structure of outer membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods. J. Mol. Biol. 190, 191-199.
    • (1986) J. Mol. Biol. , vol.190 , pp. 191-199
    • Vogel, H.1    Jähnig, F.2
  • 23
    • 0031831035 scopus 로고    scopus 로고
    • The regulated outer membrane protein Omp21 from Comamonas acidovorans is identified as a member of a new family of eight-stranded β-sheet proteins by its sequence and properties
    • 23. Baldermann, C., Lupas, A., Lubieniecki, J. & Engelhardt, H. (1998). The regulated outer membrane protein Omp21 from Comamonas acidovorans is identified as a member of a new family of eight-stranded β-sheet proteins by its sequence and properties. J. Bacteriol. 180, 3741-3749.
    • (1998) J. Bacteriol. , vol.180 , pp. 3741-3749
    • Baldermann, C.1    Lupas, A.2    Lubieniecki, J.3    Engelhardt, H.4
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • 24. Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjelgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 26
    • 0027159949 scopus 로고
    • The molecular surface package
    • 26. Connolly, M.L. (1993). The molecular surface package. J. Mol. Graph. 11, 139-141.
    • (1993) J. Mol. Graph. , vol.11 , pp. 139-141
    • Connolly, M.L.1
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • 27. Kraulis, P.J. (1991). MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • 28. Merritt, E.A. & Bacon, D.J. (1997). Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 29
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 29. Koradi, R., Billeter, M. & Wüthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.