메뉴 건너뛰기




Volumn 381, Issue 2, 2008, Pages 456-466

The Structure of an Archaeal Pilus

Author keywords

cryo EM; helical polymers; polymorphisms; quaternary structure; scanning transmission EM

Indexed keywords

GENE PRODUCT;

EID: 47049126860     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.06.017     Document Type: Article
Times cited : (43)

References (38)
  • 1
    • 33745218504 scopus 로고    scopus 로고
    • Protein secretion in the Archaea: multiple paths towards a unique cell surface
    • Albers S.V., Szabo Z., and Driessen A.J.M. Protein secretion in the Archaea: multiple paths towards a unique cell surface. Nature Rev. Microbiol. 4 (2006) 537-547
    • (2006) Nature Rev. Microbiol. , vol.4 , pp. 537-547
    • Albers, S.V.1    Szabo, Z.2    Driessen, A.J.M.3
  • 2
    • 0021763919 scopus 로고
    • Morphology, function and isolation of halobacterial flagella
    • Alam M., and Oesterhelt D. Morphology, function and isolation of halobacterial flagella. J. Mol. Biol. 176 (1984) 459-475
    • (1984) J. Mol. Biol. , vol.176 , pp. 459-475
    • Alam, M.1    Oesterhelt, D.2
  • 3
    • 0036384351 scopus 로고    scopus 로고
    • The structure of the archeabacterial flagellar filament of the extreme halophile Halobacterium salinarum R1M1 and its relation to eubacterial flagellar filaments and type IV pili
    • Cohen-Krausz S., and Trachtenberg S. The structure of the archeabacterial flagellar filament of the extreme halophile Halobacterium salinarum R1M1 and its relation to eubacterial flagellar filaments and type IV pili. J. Mol. Biol. 321 (2002) 383-395
    • (2002) J. Mol. Biol. , vol.321 , pp. 383-395
    • Cohen-Krausz, S.1    Trachtenberg, S.2
  • 4
    • 37449032773 scopus 로고    scopus 로고
    • The flagellar filament structure of the extreme acidothermophile Sulfolobus shibatae B12 suggests that archaeabacterial flagella have a unique and common symmetry and design
    • Cohen-Krausz S., and Trachtenberg S. The flagellar filament structure of the extreme acidothermophile Sulfolobus shibatae B12 suggests that archaeabacterial flagella have a unique and common symmetry and design. J. Mol. Biol. 375 (2008) 1113-1124
    • (2008) J. Mol. Biol. , vol.375 , pp. 1113-1124
    • Cohen-Krausz, S.1    Trachtenberg, S.2
  • 5
    • 0024288620 scopus 로고
    • Halobacterial flagellins are encoded by a multigene family - characterization of 5 flagellin genes
    • Gerl L., and Sumper M. Halobacterial flagellins are encoded by a multigene family - characterization of 5 flagellin genes. J. Biol. Chem. 263 (1988) 13246-13251
    • (1988) J. Biol. Chem. , vol.263 , pp. 13246-13251
    • Gerl, L.1    Sumper, M.2
  • 6
    • 0029881205 scopus 로고    scopus 로고
    • Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae
    • Jarrell K.F., Bayley D.P., Florian V., and Klein A. Isolation and characterization of insertional mutations in flagellin genes in the archaeon Methanococcus voltae. Mol. Microbiol. 20 (1996) 657-666
    • (1996) Mol. Microbiol. , vol.20 , pp. 657-666
    • Jarrell, K.F.1    Bayley, D.P.2    Florian, V.3    Klein, A.4
  • 7
    • 34247498903 scopus 로고    scopus 로고
    • Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus
    • Szabo Z., Sani M., Groeneveld M., Zolghadr B., Schelert J., Albers S.V., et al. Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus. J. Bacteriol. 189 (2007) 4305-4309
    • (2007) J. Bacteriol. , vol.189 , pp. 4305-4309
    • Szabo, Z.1    Sani, M.2    Groeneveld, M.3    Zolghadr, B.4    Schelert, J.5    Albers, S.V.6
  • 8
    • 33748757929 scopus 로고    scopus 로고
    • Archaeal flagella, bacterial flagella and type IV pili: A comparison of genes and posttranslational modifications
    • Ng S.Y.M., Chaban B., and Jarrell K.F. Archaeal flagella, bacterial flagella and type IV pili: A comparison of genes and posttranslational modifications. J. Mol. Microbiol. Biotechnol. 11 (2006) 167-191
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 167-191
    • Ng, S.Y.M.1    Chaban, B.2    Jarrell, K.F.3
  • 9
    • 0035105745 scopus 로고    scopus 로고
    • The archaeal flagellum: a different kind of prokaryotic motility structure
    • Thomas N.A., Bardy S.L., and Jarrell K.F. The archaeal flagellum: a different kind of prokaryotic motility structure. FEMS Microbiol. Rev. 25 (2001) 147-174
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 147-174
    • Thomas, N.A.1    Bardy, S.L.2    Jarrell, K.F.3
  • 10
    • 13844271970 scopus 로고    scopus 로고
    • Refining the structure of the Halobacterium salinarum flagellar filament using the iterative helical real space reconstruction method: Insights into polymorphism
    • Trachtenberg S., Galkin V.E., and Egelman E.H. Refining the structure of the Halobacterium salinarum flagellar filament using the iterative helical real space reconstruction method: Insights into polymorphism. J. Mol. Biol. 346 (2005) 665-676
    • (2005) J. Mol. Biol. , vol.346 , pp. 665-676
    • Trachtenberg, S.1    Galkin, V.E.2    Egelman, E.H.3
  • 11
    • 0023131538 scopus 로고
    • Ultrastructure and biochemistry of the cell-wall of Methanococcus voltae
    • Koval S.F., and Jarrell K.F. Ultrastructure and biochemistry of the cell-wall of Methanococcus voltae. J. Bacteriol. 169 (1987) 1298-1306
    • (1987) J. Bacteriol. , vol.169 , pp. 1298-1306
    • Koval, S.F.1    Jarrell, K.F.2
  • 12
    • 0029782668 scopus 로고    scopus 로고
    • Physiological ecology of Methanobrevibacter cuticularis sp nov and Methanobrevibacter curvatus sp nov, isolated from the hindgut of the termite Reticulitermes flavipes
    • Leadbetter J.R., and Breznak J.A. Physiological ecology of Methanobrevibacter cuticularis sp nov and Methanobrevibacter curvatus sp nov, isolated from the hindgut of the termite Reticulitermes flavipes. Appl. Environ. Microbiol. 62 (1996) 3620-3631
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3620-3631
    • Leadbetter, J.R.1    Breznak, J.A.2
  • 14
    • 33846567505 scopus 로고    scopus 로고
    • Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases
    • Szabo Z., Stahl A.O., Albers S.V., Kissinger J.C., Driessen A.J.M., and Pohlschroder M. Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases. J. Bacteriol. 189 (2007) 772-778
    • (2007) J. Bacteriol. , vol.189 , pp. 772-778
    • Szabo, Z.1    Stahl, A.O.2    Albers, S.V.3    Kissinger, J.C.4    Driessen, A.J.M.5    Pohlschroder, M.6
  • 15
    • 33745860367 scopus 로고    scopus 로고
    • Structural polymorphism in bacterial EspA filaments revealed by cryo-EM and an improved approach to helical reconstruction
    • Wang Y.A., Yu X., Yip C., Strynadka N.C., and Egelman E.H. Structural polymorphism in bacterial EspA filaments revealed by cryo-EM and an improved approach to helical reconstruction. Structure 14 (2006) 1189-1196
    • (2006) Structure , vol.14 , pp. 1189-1196
    • Wang, Y.A.1    Yu, X.2    Yip, C.3    Strynadka, N.C.4    Egelman, E.H.5
  • 16
    • 0022526226 scopus 로고
    • Mass mapping with the scanning-transmission electron-microscope
    • Wall J.S., and Hainfeld J.F. Mass mapping with the scanning-transmission electron-microscope. Annu. Rev. Biophys. Biophys. Chem. 15 (1986) 355-376
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 355-376
    • Wall, J.S.1    Hainfeld, J.F.2
  • 17
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85 (2000) 225-234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 18
    • 33845305513 scopus 로고    scopus 로고
    • The iterative helical real space reconstruction method: Surmounting the problems posed by real polymers
    • Egelman E.H. The iterative helical real space reconstruction method: Surmounting the problems posed by real polymers. J. Struct. Biol. 157 (2007) 83-94
    • (2007) J. Struct. Biol. , vol.157 , pp. 83-94
    • Egelman, E.H.1
  • 20
    • 0041620499 scopus 로고    scopus 로고
    • Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation?
    • Galkin V.E., Orlova A., VanLoock M.S., and Egelman E.H. Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation?. J. Mol. Biol. 331 (2003) 967-972
    • (2003) J. Mol. Biol. , vol.331 , pp. 967-972
    • Galkin, V.E.1    Orlova, A.2    VanLoock, M.S.3    Egelman, E.H.4
  • 23
    • 0345414561 scopus 로고    scopus 로고
    • Issues of resolution and polymorphism in single-particle reconstruction
    • Yang S.X., Yu X., Galkin V.E., and Egelman E.H. Issues of resolution and polymorphism in single-particle reconstruction. J. Struct. Biol. 144 (2003) 162-171
    • (2003) J. Struct. Biol. , vol.144 , pp. 162-171
    • Yang, S.X.1    Yu, X.2    Galkin, V.E.3    Egelman, E.H.4
  • 24
    • 33747872707 scopus 로고    scopus 로고
    • Type IV pilus structure by cryo-electron microscopy and crystallography: Implications for pilus assembly and functions
    • Craig L., Volkmann N., Arvai A.S., Pique M.E., Yeager M., Egelman E.H., and Tainer J.A. Type IV pilus structure by cryo-electron microscopy and crystallography: Implications for pilus assembly and functions. Mol. Cell 23 (2006) 651-662
    • (2006) Mol. Cell , vol.23 , pp. 651-662
    • Craig, L.1    Volkmann, N.2    Arvai, A.S.3    Pique, M.E.4    Yeager, M.5    Egelman, E.H.6    Tainer, J.A.7
  • 25
    • 0016276266 scopus 로고
    • Filamentous bacterial viruses: XIL. Molecular architecture of the class I (fd, If1, IKe) virion
    • Marvin D.A., Pigram W.J., Wiseman R.L., Wachtel E.J., and Marvin F.J. Filamentous bacterial viruses: XIL. Molecular architecture of the class I (fd, If1, IKe) virion. J. Mol. Biol. 88 (1974) 581-598
    • (1974) J. Mol. Biol. , vol.88 , pp. 581-598
    • Marvin, D.A.1    Pigram, W.J.2    Wiseman, R.L.3    Wachtel, E.J.4    Marvin, F.J.5
  • 26
    • 0015955088 scopus 로고
    • Filamentous bacterial viruses: XI. Molecular architecture of the class II (Pf1, Xf) virion
    • Marvin D.A., Wiseman R.L., and Wachtel E.J. Filamentous bacterial viruses: XI. Molecular architecture of the class II (Pf1, Xf) virion. J. Mol. Biol. 82 (1974) 121-138
    • (1974) J. Mol. Biol. , vol.82 , pp. 121-138
    • Marvin, D.A.1    Wiseman, R.L.2    Wachtel, E.J.3
  • 27
    • 0019887666 scopus 로고
    • The symmetries of filamentous phage particles
    • Caspar D.L.D., and Makowski L. The symmetries of filamentous phage particles. J. Mol. Biol. 145 (1981) 611-617
    • (1981) J. Mol. Biol. , vol.145 , pp. 611-617
    • Caspar, D.L.D.1    Makowski, L.2
  • 28
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura K., Maki-Yonekura S., and Namba K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424 (2003) 643-650
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 29
    • 15944409588 scopus 로고    scopus 로고
    • Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: a Darwinian perspective
    • Pallen M.J., Beatson S.A., and Bailey C.M. Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: a Darwinian perspective. FEMS Microbiol. Rev. 29 (2005) 201-229
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 201-229
    • Pallen, M.J.1    Beatson, S.A.2    Bailey, C.M.3
  • 31
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley L.A., MacCallum R.M., and Sternberg M.J.E. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299 (2000) 499-520
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 32
    • 20444449200 scopus 로고    scopus 로고
    • The limits of protein sequence comparison?
    • Pearson W.R., and Sierk M.L. The limits of protein sequence comparison?. Curr. Opin. Struct. Biol. 15 (2005) 254-260
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 254-260
    • Pearson, W.R.1    Sierk, M.L.2
  • 34
    • 12244298896 scopus 로고    scopus 로고
    • F-actin-like filaments formed by plasmid segregation protein ParM
    • van den E.F., Moller-Jensen J., Amos L.A., Gerdes K., and Lowe J. F-actin-like filaments formed by plasmid segregation protein ParM. EMBO J. 21 (2002) 6935-6943
    • (2002) EMBO J. , vol.21 , pp. 6935-6943
    • van den, E.F.1    Moller-Jensen, J.2    Amos, L.A.3    Gerdes, K.4    Lowe, J.5
  • 36
    • 0035868953 scopus 로고    scopus 로고
    • Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling
    • Samatey F.A., Imada K., Nagashima S., Vonderviszt F., Kumasaka T., Yamamoto M., and Namba K. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature 410 (2001) 331-337
    • (2001) Nature , vol.410 , pp. 331-337
    • Samatey, F.A.1    Imada, K.2    Nagashima, S.3    Vonderviszt, F.4    Kumasaka, T.5    Yamamoto, M.6    Namba, K.7
  • 37
    • 0023990563 scopus 로고
    • Isolation of flagella from the archaebacterium Methanococcus voltae by phase-separation with Triton X-114
    • Kalmokoff M.L., Jarrell K.F., and Koval S.F. Isolation of flagella from the archaebacterium Methanococcus voltae by phase-separation with Triton X-114. J. Bacteriol. 170 (1988) 1752-1758
    • (1988) J. Bacteriol. , vol.170 , pp. 1752-1758
    • Kalmokoff, M.L.1    Jarrell, K.F.2    Koval, S.F.3
  • 38
    • 34247093347 scopus 로고    scopus 로고
    • Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked beta-solenoid model of HET-s prion fibrils
    • Sen A., Baxa U., Simon M.N., Wall J.S., Sabate R., Saupe S.J., and Steven A.C. Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked beta-solenoid model of HET-s prion fibrils. J. Biol. Chem. 282 (2007) 5545-5550
    • (2007) J. Biol. Chem. , vol.282 , pp. 5545-5550
    • Sen, A.1    Baxa, U.2    Simon, M.N.3    Wall, J.S.4    Sabate, R.5    Saupe, S.J.6    Steven, A.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.