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Volumn 107, Issue 3, 2010, Pages 1065-1070

Erratum: Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility (Proceedings of the National Academy of Sciences of the United States of America (2010) 107, 3 (1065-1070) DOI:10.1073/pnas.0911616107);Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility

Author keywords

Calcium binding; Human pathogen; Microbiology; Pilus biogenesis; Structural biology

Indexed keywords

BACTERIAL PROTEIN; CALCIUM; LYSINE; PROTEIN PILY1; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 75749098143     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1000441107     Document Type: Erratum
Times cited : (75)

References (35)
  • 1
    • 41949117894 scopus 로고    scopus 로고
    • Type IV pili: Paradoxes in form and function
    • Craig L, Li J (2008) Type IV pili: Paradoxes in form and function. Curr Opin Struct Biol, 18:267-277.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 267-277
    • Craig, L.1    Li, J.2
  • 2
    • 0034618643 scopus 로고    scopus 로고
    • Pilus retraction powers bacterial twitching motility
    • Merz AJ, So M, Sheetz MP (2000) Pilus retraction powers bacterial twitching motility. Nature, 407:98-102.
    • (2000) Nature , vol.407 , pp. 98-102
    • Merz, A.J.1    So, M.2    Sheetz, M.P.3
  • 3
    • 0035810950 scopus 로고    scopus 로고
    • Direct observation of extension and retraction of type IV pili
    • Skerker JM, Berg HC (2001) Direct observation of extension and retraction of type IV pili. Proc Natl Acad Sci USA, 98:6901-6904.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6901-6904
    • Skerker, J.M.1    Berg, H.C.2
  • 4
    • 0031824719 scopus 로고    scopus 로고
    • PilT mutations lead to simultaneous defects in competence for natural transformation and twitching motility in piliated Neisseria gonorrhoeae
    • Wolfgang M, et al. (1998) PilT mutations lead to simultaneous defects in competence for natural transformation and twitching motility in piliated Neisseria gonorrhoeae. Mol Microbiol, 29:321-330.
    • (1998) Mol Microbiol , vol.29 , pp. 321-330
    • Wolfgang, M.1
  • 5
    • 0032968052 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa gene products PilT and PilU are required for cytotoxicity in vitro and virulence in a mouse model of acute pneumonia
    • Comolli JC, et al. (1999) Pseudomonas aeruginosa gene products PilT and PilU are required for cytotoxicity in vitro and virulence in a mouse model of acute pneumonia. Infect Immun, 67:3625-3630.
    • (1999) Infect Immun , vol.67 , pp. 3625-3630
    • Comolli, J.C.1
  • 6
    • 0036405357 scopus 로고    scopus 로고
    • Type IV pili and twitching motility
    • Mattick JS (2002) Type IV pili and twitching motility. Annu Rev Microbiol, 56:289-314.
    • (2002) Annu Rev Microbiol , vol.56 , pp. 289-314
    • Mattick, J.S.1
  • 7
    • 0028920724 scopus 로고
    • Role of Pseudomonas aeruginosa pili in acute pulmonary infection
    • Tang H, Kays M, Prince A (1995) Role of Pseudomonas aeruginosa pili in acute pulmonary infection. Infect Immun, 63:1278-1285.
    • (1995) Infect Immun , vol.63 , pp. 1278-1285
    • Tang, H.1    Kays, M.2    Prince, A.3
  • 8
    • 38849174766 scopus 로고    scopus 로고
    • Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosatype IV pilus motor proteins PilB, PilT and PilU
    • Chiang P, et al. (2008) Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosatype IV pilus motor proteins PilB, PilT and PilU. Microbiology, 154:114-126.
    • (2008) Microbiology , vol.154 , pp. 114-126
    • Chiang, P.1
  • 9
    • 41549119041 scopus 로고    scopus 로고
    • PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus
    • Jakovljevic V, Leonardy S, Hoppert M, Sogaard-Andersen L (2008) PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus. J Bacteriol, 190:2411-2421.
    • (2008) J Bacteriol , vol.190 , pp. 2411-2421
    • Jakovljevic, V.1    Leonardy, S.2    Hoppert, M.3    Sogaard-Andersen, L.4
  • 10
    • 0027208681 scopus 로고
    • Mutations in the consensus ATP-binding sites of XcpR and PilB eliminate extracellular protein secretion and pilus biogenesis in Pseudomonas aeruginosa
    • Turner LR, Lara JC, Nunn DN, Lory S (1993) Mutations in the consensus ATP-binding sites of XcpR and PilB eliminate extracellular protein secretion and pilus biogenesis in Pseudomonas aeruginosa. J Bacteriol, 175:4962-4969.
    • (1993) J Bacteriol , vol.175 , pp. 4962-4969
    • Turner, L.R.1    Lara, J.C.2    Nunn, D.N.3    Lory, S.4
  • 11
    • 3142631733 scopus 로고    scopus 로고
    • Type IV pilus retraction in pathogenic Neisseria is regulated by the PilC proteins
    • Morand PC, et al. (2004) Type IV pilus retraction in pathogenic Neisseria is regulated by the PilC proteins. Embo J, 23:2009-2017.
    • (2004) Embo J , vol.23 , pp. 2009-2017
    • Morand, P.C.1
  • 12
    • 0025878130 scopus 로고
    • Characterisation of a Pseudomonas aeruginosatwitching motility gene and evidence for a specialised protein export system widespread in eubacteria
    • Whitchurch CB, et al. (1991) Characterisation of a Pseudomonas aeruginosatwitching motility gene and evidence for a specialised protein export system widespread in eubacteria. Gene, 101:33-44.
    • (1991) Gene , vol.101 , pp. 33-44
    • Whitchurch, C.B.1
  • 13
    • 0029797933 scopus 로고    scopus 로고
    • Fimbrial biogenesis genes of Pseudomonas aeruginosa: PilW and pilX increase the similarity of type 4 fimbriae to the GSP protein-secretion systems and pilY1 encodes a gonococcal PilC homologue
    • Alm RA, Hallinan JP, Watson AA, Mattick JS (1996) Fimbrial biogenesis genes of Pseudomonas aeruginosa: pilW and pilX increase the similarity of type 4 fimbriae to the GSP protein-secretion systems and pilY1 encodes a gonococcal PilC homologue. Mol Microbiol, 22:161-173.
    • (1996) Mol Microbiol , vol.22 , pp. 161-173
    • Alm, R.A.1    Hallinan, J.P.2    Watson, A.A.3    Mattick, J.S.4
  • 14
    • 0028795092 scopus 로고
    • Neisseria PilC protein identified as type-4 pilus tip-located adhesin
    • Rudel T, Scheurerpflug I, Meyer TF (1995) Neisseria PilC protein identified as type-4 pilus tip-located adhesin. Nature, 373:357-359.
    • (1995) Nature , vol.373 , pp. 357-359
    • Rudel, T.1    Scheurerpflug, I.2    Meyer, T.F.3
  • 15
    • 0032409987 scopus 로고    scopus 로고
    • Suppression of an absolute defect in type IV pilus biogenesis by loss-of-function mutations in pilT, a twitching motility gene in Neisseria gonorrhoeae
    • Wolfgang M, et al. (1998) Suppression of an absolute defect in type IV pilus biogenesis by loss-of-function mutations in pilT, a twitching motility gene in Neisseria gonorrhoeae. Proc Natl Acad Sci USA, 95:14973-14978.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14973-14978
    • Wolfgang, M.1
  • 16
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley LA, Sternberg MJ (2009) Protein structure prediction on the Web: A case study using the Phyre server. Nat Protoc, 4:363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 17
    • 0032127358 scopus 로고    scopus 로고
    • The biology workbench - A seamless database and analysis environment for the biologist
    • Subramaniam S (1998) The biology workbench - A seamless database and analysis environment for the biologist. Proteins, 32:1-2.
    • (1998) Proteins , vol.32 , pp. 1-2
    • Subramaniam, S.1
  • 18
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson WA, Horton JR, LeMaster DM (1990) Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure. Embo J, 9:1665-1672.
    • (1990) Embo J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 22
    • 0028303437 scopus 로고
    • High level expression in Escherichia coli and characterization of the EF-hand calcium-binding protein caltractin
    • Weber C, Lee VD, Chazin WJ, Huang B (1994) High level expression in Escherichia coli and characterization of the EF-hand calcium-binding protein caltractin. J Biol Chem, 269:15795-15802.
    • (1994) J Biol Chem , vol.269 , pp. 15795-15802
    • Weber, C.1    Lee, V.D.2    Chazin, W.J.3    Huang, B.4
  • 23
    • 0021895143 scopus 로고
    • 2+ of catalytic activity of the superoxide-producing NADPH oxidase in membrane fractions of human neutrophils and monocytes
    • 2+ of catalytic activity of the superoxide-producing NADPH oxidase in membrane fractions of human neutrophils and monocytes. J Biol Chem, 260:3635-3639.
    • (1985) J Biol Chem , vol.260 , pp. 3635-3639
    • Suzuki, H.1    Pabst, M.J.2    Johnston Jr, R.B.3
  • 24
    • 70350008224 scopus 로고    scopus 로고
    • Calcium is essential for the major pseudopilin in the type 2 secretion system
    • Korotkov KV, et al. (2009) Calcium is essential for the major pseudopilin in the type 2 secretion system. J Biol Chem, 284:25466-25470.
    • (2009) J Biol Chem , vol.284 , pp. 25466-25470
    • Korotkov, K.V.1
  • 25
    • 0037058989 scopus 로고    scopus 로고
    • Single pilus motor forces exceed 100 pN
    • Maier B, et al. (2002) Single pilus motor forces exceed 100 pN. Proc Natl Acad Sci USA, 99:16012-16017.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16012-16017
    • Maier, B.1
  • 26
    • 3342922288 scopus 로고    scopus 로고
    • A force-dependent switch reverses type IV pilus retraction
    • SheetzMP
    • Maier B, Koomey M, SheetzMP (2004) A force-dependent switch reverses type IV pilus retraction. Proc Natl Acad Sci USA, 101:10961-10966.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10961-10966
    • Maier, B.1    Koomey, M.2
  • 27
    • 0028100375 scopus 로고
    • Alteration of the pilin adhesin of Pseudomonas aeruginosa PAO results in normal pilus biogenesis but a loss of adherence to human pneumocyte cells and decreased virulence in mice
    • Farinha MA, et al. (1994) Alteration of the pilin adhesin of Pseudomonas aeruginosa PAO results in normal pilus biogenesis but a loss of adherence to human pneumocyte cells and decreased virulence in mice. Infect Immun, 62:4118-4123.
    • (1994) Infect Immun , vol.62 , pp. 4118-4123
    • Farinha, M.A.1
  • 28
    • 33646088314 scopus 로고    scopus 로고
    • Catch-bond model derived from allostery explains forceactivated bacterial adhesion
    • Thomas W, et al. (2006) Catch-bond model derived from allostery explains forceactivated bacterial adhesion. Biophys J, 90:753-764.
    • (2006) Biophys J , vol.90 , pp. 753-764
    • Thomas, W.1
  • 29
    • 53349117639 scopus 로고    scopus 로고
    • Catch-bond mechanism of force-enhanced adhesion: Counterintuitive, elusive, but... widespread?
    • Sokurenko EV, Vogel V, Thomas WE (2008) Catch-bond mechanism of force-enhanced adhesion: Counterintuitive, elusive, but... widespread?. Cell Host Microbe, 4:314-323.
    • (2008) Cell Host Microbe , vol.4 , pp. 314-323
    • Sokurenko, E.V.1    Vogel, V.2    Thomas, W.E.3
  • 30
    • 17644417153 scopus 로고    scopus 로고
    • CD46-independent binding of neisserial type IV pili and the major pilus adhesin, PilC, to human epithelial cells
    • Kirchner M, Heuer D, Meyer TF (2005) CD46-independent binding of neisserial type IV pili and the major pilus adhesin, PilC, to human epithelial cells. Infect Immun, 73:3072-3082.
    • (2005) Infect Immun , vol.73 , pp. 3072-3082
    • Kirchner, M.1    Heuer, D.2    Meyer, T.F.3
  • 31
    • 0030779080 scopus 로고    scopus 로고
    • Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria
    • Kallstrom H, Liszewski MK, Atkinson JP, Jonsson AB (1997) Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria. Mol Microbiol, 25:639-647.
    • (1997) Mol Microbiol , vol.25 , pp. 639-647
    • Kallstrom, H.1    Liszewski, M.K.2    Atkinson, J.P.3    Jonsson, A.B.4
  • 32
    • 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
  • 33
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - from diffraction images to an initial model in minutes
    • Minor W, Cymborowski M, Otwinowski Z, Chruszcz M (2006) HKL-3000: The integration of data reduction and structure solution - from diffraction images to an initial model in minutes. Acta Crystallogr D, 62:859-866.
    • (2006) Acta Crystallogr D , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 34
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Cowtan PEaK (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D, 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Cowtan, P.E.K.1
  • 35
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D, 54:905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brunger, A.T.1


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