메뉴 건너뛰기




Volumn 422, Issue 2, 2012, Pages 274-281

Filaments from ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices

Author keywords

archaea; convergent evolution; electron microscopy; helical polymers

Indexed keywords

BACTERIAL PROTEIN; FLAGELLIN; PILIN;

EID: 84864853841     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.05.031     Document Type: Article
Times cited : (28)

References (58)
  • 1
    • 0014889416 scopus 로고
    • Polymerization of flagellin and polymorphism of flagella
    • S. Asakura Polymerization of flagellin and polymorphism of flagella Adv. Biophys. 1 1970 99 155
    • (1970) Adv. Biophys. , vol.1 , pp. 99-155
    • Asakura, S.1
  • 2
    • 0025896303 scopus 로고
    • A molecular switch: Subunit rotations involved in the right-handed to left-handed transitions of Salmonella typhimurium flagellar filaments
    • S. Trachtenberg, and D.J. DeRosier A molecular switch: subunit rotations involved in the right-handed to left-handed transitions of Salmonella typhimurium flagellar filaments J. Mol. Biol. 220 1991 67 77 (Pubitemid 121004543)
    • (1991) Journal of Molecular Biology , vol.220 , Issue.1 , pp. 67-77
    • Trachtenberg, S.1    DeRosier, D.J.2
  • 3
    • 0025823676 scopus 로고
    • Point mutations that lock Salmonella typhimurium flagellar filaments in the straight right-handed and left-handed forms and their relation to filament superhelicity
    • H.C. Hyman, and S. Trachtenberg Point mutations that lock Salmonella typhimurium flagellar filaments in the straight right-handed and left-handed forms and their relation to filament superhelicity J. Mol. Biol. 220 1991 79 88 (Pubitemid 121004544)
    • (1991) Journal of Molecular Biology , vol.220 , Issue.1 , pp. 79-88
    • Hyman, H.C.1    Trachtenberg, S.2
  • 4
    • 0018940149 scopus 로고
    • Formation of helical filaments by copolymerization of two types of 'straight' flagellins
    • DOI 10.1038/286628a0
    • R. Kamiya, S. Asakura, and S. Yamaguchi Formation of helical filaments by copolymerization of two types of 'straight' flagellins Nature 286 1980 628 630 (Pubitemid 10015376)
    • (1980) Nature , vol.286 , Issue.5773 , pp. 628-630
    • Kamiya, R.1    Asakura, S.2    Yamaguchi, S.3
  • 5
    • 0017166951 scopus 로고
    • Flagellar transformations at alkaline pH
    • R. Kamiya, and S. Asakura Flagellar transformations at alkaline pH J. Mol. Biol. 108 1976 513 518
    • (1976) J. Mol. Biol. , vol.108 , pp. 513-518
    • Kamiya, R.1    Asakura, S.2
  • 6
    • 0017138443 scopus 로고
    • Helical transformations of Salmonella flagella in vitro
    • R. Kamiya, and S. Asakura Helical transformations of Salmonella flagella in vitro J. Mol. Biol. 106 1976 167 186
    • (1976) J. Mol. Biol. , vol.106 , pp. 167-186
    • Kamiya, R.1    Asakura, S.2
  • 7
    • 0013894066 scopus 로고
    • Salmonella flagella: In vitro reconstruction and over-all shapes of flagellar filaments
    • S. Asakura, G. Eguchi, and T. Iino Salmonella flagella: in vitro reconstruction and over-all shapes of flagellar filaments J. Mol. Biol. 16 1966 302 316
    • (1966) J. Mol. Biol. , vol.16 , pp. 302-316
    • Asakura, S.1    Eguchi, G.2    Iino, T.3
  • 8
    • 0017841508 scopus 로고
    • Change of waveform in bacterial flagella: The role of mechanics at the molecular level
    • C.R. Calladine Change of waveform in bacterial flagella: the role of mechanics at the molecular level J. Mol. Biol. 118 1978 457 479 (Pubitemid 8271376)
    • (1978) Journal of Molecular Biology , vol.118 , Issue.4 , pp. 457-479
    • Calladine, C.R.1
  • 9
    • 0016770351 scopus 로고
    • Construction of bacterial flagella
    • C.R. Calladine Construction of bacterial flagella Nature 255 1975 121 124
    • (1975) Nature , vol.255 , pp. 121-124
    • Calladine, C.R.1
  • 10
    • 0031982793 scopus 로고    scopus 로고
    • Quasi- and nonequivalence in the structure of bacterial flagellar filament
    • K. Hasegawa, I. Yamashita, and K. Namba Quasi- and nonequivalence in the structure of bacterial flagellar filament Biophys. J. 74 1998 569 575 (Pubitemid 28041784)
    • (1998) Biophysical Journal , vol.74 , Issue.1 , pp. 569-575
    • Hasegawa, K.1    Yamashita, I.2    Namba, K.3
  • 11
    • 77950477195 scopus 로고    scopus 로고
    • Conformational change of flagellin for polymorphic supercoiling of the flagellar filament
    • S. Maki-Yonekura, K. Yonekura, and K. Namba Conformational change of flagellin for polymorphic supercoiling of the flagellar filament Nat. Struct. Mol. Biol. 17 2010 417 422
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 417-422
    • Maki-Yonekura, S.1    Yonekura, K.2    Namba, K.3
  • 12
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • DOI 10.1038/nature01830
    • K. Yonekura, S. Maki-Yonekura, and K. Namba Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy Nature 424 2003 643 650 (Pubitemid 36987983)
    • (2003) Nature , vol.424 , Issue.6949 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 13
    • 0035868953 scopus 로고    scopus 로고
    • Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling
    • DOI 10.1038/35066504
    • F.A. Samatey, K. Imada, S. Nagashima, F. Vonderviszt, T. Kumasaka, M. Yamamoto, and K. Namba Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling Nature 410 2001 331 337 (Pubitemid 32246042)
    • (2001) Nature , vol.410 , Issue.6826 , 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
  • 14
  • 15
    • 42349084254 scopus 로고    scopus 로고
    • Divergence of quaternary structures among bacterial flagellar filaments
    • DOI 10.1126/science.1155307
    • V.E. Galkin, X. Yu, J. Bielnicki, J. Heuser, C.P. Ewing, P. Guerry, and E.H. Egelman Divergence of quaternary structures among bacterial flagellar filaments Science 320 2008 382 385 (Pubitemid 351555662)
    • (2008) Science , vol.320 , Issue.5874 , pp. 382-385
    • Galkin, V.E.1    Yu, X.2    Bielnicki, J.3    Heuser, J.4    Ewing, C.P.5    Guerry, P.6    Egelman, E.H.7
  • 17
    • 0025988180 scopus 로고
    • Role of the disordered terminal regions of flagellin in filament formation and stability
    • F. Vonderviszt, S. Aizawa, and K. Namba Role of the disordered terminal regions of flagellin in filament formation and stability J. Mol. Biol. 221 1991 1461 1474 (Pubitemid 121003466)
    • (1991) Journal of Molecular Biology , vol.221 , Issue.4 , pp. 1461-1474
    • Vonderviszt, F.1    Aizawa, S.-I.2    Namba, K.3
  • 18
    • 0035213102 scopus 로고    scopus 로고
    • Characterization of flagellum gene families of methanogenic archaea and localization of novel flagellum accessory proteins
    • DOI 10.1128/JB.183.24.7154-7164.2001
    • N.A. Thomas, and K.F. Jarrell Characterization of flagellum gene families of methanogenic archaea and localization of novel flagellum accessory proteins J. Bacteriol. 183 2001 7154 7164 (Pubitemid 33121849)
    • (2001) Journal of Bacteriology , vol.183 , Issue.24 , pp. 7154-7164
    • Thomas, N.A.1    Jarrell, K.F.2
  • 19
    • 0035105745 scopus 로고    scopus 로고
    • The archaeal flagellum: A different kind of prokaryotic motility structure
    • DOI 10.1016/S0168-6445(00)00061-9, PII S0168644500000619
    • N.A. Thomas, S.L. Bardy, and K.F. Jarrell The archaeal flagellum: a different kind of prokaryotic motility structure FEMS Microbiol. Rev. 25 2001 147 174 (Pubitemid 32201980)
    • (2001) FEMS Microbiology Reviews , vol.25 , Issue.2 , pp. 147-174
    • Thomas, N.A.1    Bardy, S.L.2    Jarrell, K.F.3
  • 20
    • 0034888193 scopus 로고    scopus 로고
    • Insertional inactivation of the flaH gene in the archaeon Methanococcus voltae results in non-flagellated cells
    • DOI 10.1007/s004380100451
    • N.A. Thomas, C.T. Pawson, and K.F. Jarrell Insertional inactivation of the flaH gene in the archaeon Methanococcus voltae results in non-flagellated cells Mol. Genet. Genomics 265 2001 596 603 (Pubitemid 32763312)
    • (2001) Molecular Genetics and Genomics , vol.265 , Issue.4 , pp. 596-603
    • Thomas, N.A.1    Pawson, C.T.2    Jarrell, K.F.3
  • 21
    • 0032014974 scopus 로고    scopus 로고
    • Further evidence to suggest that archaeal flagella are related to bacterial type IV pili
    • D.P. Bayley, and K.F. Jarrell Further evidence to suggest that archaeal flagella are related to bacterial type IV pili J. Mol. Evol. 46 1998 370 373
    • (1998) J. Mol. Evol. , vol.46 , pp. 370-373
    • Bayley, D.P.1    Jarrell, K.F.2
  • 22
    • 33846567505 scopus 로고    scopus 로고
    • Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases
    • DOI 10.1128/JB.01547-06
    • Z. Szabo, A.O. Stahl, S.V. Albers, J.C. Kissinger, A.J. Driessen, and M. Pohlschroder Identification of diverse archaeal proteins with class III signal peptides cleaved by distinct archaeal prepilin peptidases J. Bacteriol. 189 2007 772 778 (Pubitemid 46183851)
    • (2007) Journal of Bacteriology , vol.189 , Issue.3 , 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
  • 23
    • 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
    • DOI 10.1016/j.jmb.2007.10.048, PII S0022283607013848
    • S. Cohen-Krausz, and S. Trachtenberg 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 (Pubitemid 50009428)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.4 , pp. 1113-1124
    • Cohen-Krausz, S.1    Trachtenberg, S.2
  • 24
    • 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
    • DOI 10.1016/j.jmb.2004.12.010
    • S. Trachtenberg, V.E. Galkin, and E.H. Egelman 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 (Pubitemid 40247709)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.3 , pp. 665-676
    • Trachtenberg, S.1    Galkin, V.E.2    Egelman, E.H.3
  • 25
    • 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
    • S. Cohen-Krausz, and S. Trachtenberg 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
  • 26
    • 33747872707 scopus 로고    scopus 로고
    • Type IV Pilus Structure by Cryo-Electron Microscopy and Crystallography: Implications for Pilus Assembly and Functions
    • DOI 10.1016/j.molcel.2006.07.004, PII S1097276506004813
    • L. Craig, N. Volkmann, A.S. Arvai, M.E. Pique, M. Yeager, E.H. Egelman, and J.A. Tainer Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions Mol. Cell 23 2006 651 662 (Pubitemid 44292553)
    • (2006) Molecular Cell , vol.23 , Issue.5 , pp. 651-662
    • Craig, L.1    Volkmann, N.2    Arvai, A.S.3    Pique, M.E.4    Yeager, M.5    Egelman, EdwardH.6    Tainer, J.A.7
  • 27
    • 0031006047 scopus 로고    scopus 로고
    • Type-4 pilus-structure: Outside to inside and top to bottom - A minireview
    • DOI 10.1016/S0378-1119(97)00008-5, PII S0378111997000085
    • K.T. Forest, and J.A. Tainer Type-4 pilus-structure: outside to inside and top to bottom - a minireview Gene 192 1997 165 169 (Pubitemid 27267491)
    • (1997) Gene , vol.192 , Issue.1 , pp. 165-169
    • Forest, K.T.1    Tainer, J.A.2
  • 29
    • 42649085698 scopus 로고    scopus 로고
    • Type IV pili: e pluribus unum?
    • DOI 10.1111/j.1365-2958.2008.06197.x
    • V. Pelicic Type IV pili: e pluribus unum? Mol. Microbiol. 68 2008 827 837 (Pubitemid 351596335)
    • (2008) Molecular Microbiology , vol.68 , Issue.4 , pp. 827-837
    • Pelicic, V.1
  • 30
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • DOI 10.1038/nrmicro885
    • L. Craig, M.E. Pique, and J.A. Tainer Type IV pilus structure and bacterial pathogenicity Nat. Rev. Microbiol. 2 2004 363 378 (Pubitemid 39490116)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.5 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 31
    • 0038170287 scopus 로고    scopus 로고
    • Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity
    • DOI 10.1128/JB.185.13.3918-3925.2003
    • S.V. Albers, Z. Szabo, and A.J. Driessen Archaeal homolog of bacterial type IV prepilin signal peptidases with broad substrate specificity J. Bacteriol. 185 2003 3918 3925 (Pubitemid 36735943)
    • (2003) Journal of Bacteriology , vol.185 , Issue.13 , pp. 3918-3925
    • Albers, S.-V.1    Szabo, Z.2    Driessen, A.J.M.3
  • 32
    • 79958816876 scopus 로고    scopus 로고
    • Archaeal type IV pilus-like structures - Evolutionarily conserved prokaryotic surface organelles
    • M. Pohlschroder, A. Ghosh, M. Tripepi, and S.V. Albers Archaeal type IV pilus-like structures - evolutionarily conserved prokaryotic surface organelles Curr. Opin. Microbiol. 14 2011 357 363
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 357-363
    • Pohlschroder, M.1    Ghosh, A.2    Tripepi, M.3    Albers, S.V.4
  • 33
    • 70350455958 scopus 로고    scopus 로고
    • The Iho670 fibers of Ignicoccus hospitalis: A new type of archaeal cell surface appendage
    • D.W. Müller, C. Meyer, S. Gürster, U. Küper, H. Huber, and R. Rachel The Iho670 fibers of Ignicoccus hospitalis: a new type of archaeal cell surface appendage J. Bacteriol. 191 2009 6465 6468
    • (2009) J. Bacteriol. , vol.191 , pp. 6465-6468
    • Müller, D.W.1    Meyer, C.2    Gürster, S.3    Küper, U.4    Huber, H.5    Rachel, R.6
  • 34
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 35
    • 33646014793 scopus 로고    scopus 로고
    • Variation in bacterial flagellins: From sequence to structure
    • S.A. Beatson, T. Minamino, and M.J. Pallen Variation in bacterial flagellins: from sequence to structure Trends Microbiol. 14 2006 151 155
    • (2006) Trends Microbiol. , vol.14 , pp. 151-155
    • Beatson, S.A.1    Minamino, T.2    Pallen, M.J.3
  • 36
    • 33748773323 scopus 로고    scopus 로고
    • Type IV pilin structures: Insights on shared architecture, fiber assembly, receptor binding and type II secretion
    • DOI 10.1159/000094054
    • J.K. Hansen, and K.T. Forest Type IV pilin structures: insights on shared architecture, fiber assembly, receptor binding and type II secretion J. Mol. Microbiol. Biotechnol. 11 2006 192 207 (Pubitemid 44414055)
    • (2006) Journal of Molecular Microbiology and Biotechnology , vol.11 , Issue.3-5 , pp. 192-207
    • Hansen, J.K.1    Forest, K.T.2
  • 38
    • 0030596081 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA deposited onto mica: Equilibration versus kinetic trapping studied by statistical polymer chain analysis
    • DOI 10.1006/jmbi.1996.0687
    • C. Rivetti, M. Guthold, and C. Bustamante Scanning force microscopy of DNA deposited onto mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis J. Mol. Biol. 264 1996 919 932 (Pubitemid 27019483)
    • (1996) Journal of Molecular Biology , vol.264 , Issue.5 , pp. 919-932
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 39
    • 77955270274 scopus 로고    scopus 로고
    • Helical filaments of human Dmc1 protein on single-stranded DNA: A cautionary tale
    • X. Yu, and E.H. Egelman Helical filaments of human Dmc1 protein on single-stranded DNA: a cautionary tale J. Mol. Biol. 401 2010 544 551
    • (2010) J. Mol. Biol. , vol.401 , pp. 544-551
    • Yu, X.1    Egelman, E.H.2
  • 40
    • 77957320447 scopus 로고    scopus 로고
    • Reconstruction of helical filaments and tubes
    • E.H. Egelman Reconstruction of helical filaments and tubes Methods Enzymol. 482 2010 167 183
    • (2010) Methods Enzymol. , vol.482 , pp. 167-183
    • Egelman, E.H.1
  • 41
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • E.H. Egelman 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
  • 42
    • 77955628595 scopus 로고    scopus 로고
    • Detailed structural and assembly model of the type II secretion pilus from sparse data
    • M. Campos, M. Nilges, D.A. Cisneros, and O. Francetic Detailed structural and assembly model of the type II secretion pilus from sparse data Proc. Natl Acad. Sci. USA 107 2010 13081 13086
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 13081-13086
    • Campos, M.1    Nilges, M.2    Cisneros, D.A.3    Francetic, O.4
  • 43
    • 0345414561 scopus 로고    scopus 로고
    • Issues of resolution and polymorphism in single-particle reconstruction
    • DOI 10.1016/j.jsb.2003.09.016
    • S. Yang, X. Yu, V.E. Galkin, and E.H. Egelman Issues of resolution and polymorphism in single-particle reconstruction J. Struct. Biol. 144 2003 162 171 (Pubitemid 37468375)
    • (2003) Journal of Structural Biology , vol.144 , Issue.1-2 , pp. 162-171
    • Yang, S.1    Yu, X.2    Galkin, V.E.3    Egelman, E.H.4
  • 44
    • 0033777020 scopus 로고    scopus 로고
    • Resolution measurement in structures derived from single particles
    • N. Grigorieff Resolution measurement in structures derived from single particles Acta Crystallogr. D Biol. Crystallogr. 56 Pt 10 2000 1270 1277
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , Issue.PART 10 , pp. 1270-1277
    • Grigorieff, N.1
  • 45
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • DOI 10.1016/j.jmb.2003.07.013
    • P.B. Rosenthal, and R. Henderson Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy J. Mol. Biol. 333 2003 721 745 (Pubitemid 37268015)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 47
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • DOI 10.1006/jmbi.1999.3091
    • D.T. Jones Protein secondary structure prediction based on position-specific scoring matrices J. Mol. Biol. 292 1999 195 202 (Pubitemid 29435759)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 195-202
    • Jones, D.T.1
  • 50
    • 36749078686 scopus 로고    scopus 로고
    • Combining Efficient Conformational Sampling with a Deformable Elastic Network Model Facilitates Structure Refinement at Low Resolution
    • DOI 10.1016/j.str.2007.09.021, PII S096921260700411X
    • G.F. Schröder, A.T. Brunger, and M. Levitt Combining efficient conformational sampling with a deformable elastic network model facilitates structure refinement at low resolution Structure 15 2007 1630 1641 (Pubitemid 350213409)
    • (2007) Structure , vol.15 , Issue.12 , pp. 1630-1641
    • Schroder, G.F.1    Brunger, A.T.2    Levitt, M.3
  • 51
    • 69849107000 scopus 로고    scopus 로고
    • Structural polymorphism of the ParM filament and dynamic instability
    • V.E. Galkin, A. Orlova, C. Rivera, R.D. Mullins, and E.H. Egelman Structural polymorphism of the ParM filament and dynamic instability Structure 17 2009 1253 1264
    • (2009) Structure , vol.17 , pp. 1253-1264
    • Galkin, V.E.1    Orlova, A.2    Rivera, C.3    Mullins, R.D.4    Egelman, E.H.5
  • 52
    • 69849097861 scopus 로고    scopus 로고
    • The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation
    • J.K. Polka, J.M. Kollman, D.A. Agard, and R.D. Mullins The structure and assembly dynamics of plasmid actin AlfA imply a novel mechanism of DNA segregation J. Bacteriol. 191 2009 6219 6230
    • (2009) J. Bacteriol. , vol.191 , pp. 6219-6230
    • Polka, J.K.1    Kollman, J.M.2    Agard, D.A.3    Mullins, R.D.4
  • 54
    • 77950020896 scopus 로고    scopus 로고
    • Polymeric structures and dynamic properties of the bacterial actin AlfA
    • D. Popp, A. Narita, U. Ghoshdastider, K. Maeda, Y. Maeda, and T. Oda Polymeric structures and dynamic properties of the bacterial actin AlfA J. Mol. Biol. 397 2010 1031 1041
    • (2010) J. Mol. Biol. , vol.397 , pp. 1031-1041
    • Popp, D.1    Narita, A.2    Ghoshdastider, U.3    Maeda, K.4    Maeda, Y.5    Oda, T.6
  • 55
    • 77951220899 scopus 로고    scopus 로고
    • Structure and filament dynamics of the pSK41 actin-like ParM protein: Implications for plasmid DNA segregation
    • D. Popp, W. Xu, A. Narita, A.J. Brzoska, R.A. Skurray, and N. Firth Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation J. Biol. Chem. 285 2010 10130 10140
    • (2010) J. Biol. Chem. , vol.285 , pp. 10130-10140
    • Popp, D.1    Xu, W.2    Narita, A.3    Brzoska, A.J.4    Skurray, R.A.5    Firth, N.6
  • 57
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • S.J. Ludtke, P.R. Baldwin, and W. Chiu EMAN: semiautomated software for high-resolution single-particle reconstructions J. Struct. Biol. 128 1999 82 97 (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 58
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • DOI 10.1006/jsbi.1996.0030
    • J. Frank, M. Radermacher, P. Penczek, J. Zhu, Y. Li, M. Ladjadj, and A. Leith SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116 1996 190 199 (Pubitemid 26093143)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.