메뉴 건너뛰기




Volumn 381, Issue 1, 2008, Pages 189-199

Crystal Structure of the C-Terminal Domain of a Flagellar Hook-Capping Protein from Xanthomonas campestris

Author keywords

FlgD; hook capping; Ig like domain; Tudor like domain; Xanthomonas campestris

Indexed keywords

AMINO ACID; BACTERIAL PROTEIN; DIMER; FIBRONECTIN; FIBRONECTIN TYPE III; MONOMER;

EID: 46649102824     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.05.083     Document Type: Article
Times cited : (18)

References (50)
  • 1
    • 0032698478 scopus 로고    scopus 로고
    • The bacterial flagellum: reversible rotary propellor and type III export apparatus
    • Macnab R.M. The bacterial flagellum: reversible rotary propellor and type III export apparatus. J. Bacteriol. 181 (1999) 7149-7153
    • (1999) J. Bacteriol. , vol.181 , pp. 7149-7153
    • Macnab, R.M.1
  • 2
    • 16244411638 scopus 로고    scopus 로고
    • Bacterial flagellar diversity in the post-genomic era
    • Pallen M.J., Penn C.W., and Chaudhuri R.R. Bacterial flagellar diversity in the post-genomic era. Trends Microbiol. 13 (2005) 143-149
    • (2005) Trends Microbiol. , vol.13 , pp. 143-149
    • Pallen, M.J.1    Penn, C.W.2    Chaudhuri, R.R.3
  • 3
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab R.M. How bacteria assemble flagella. Annu. Rev. Microbiol. 57 (2003) 77-100
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 4
    • 0023128224 scopus 로고
    • Rapid rotation of flagellar bundles in swimming bacteria
    • Lowe G., Meiser M., and Berg H.C. Rapid rotation of flagellar bundles in swimming bacteria. Nature 325 (1987) 637-640
    • (1987) Nature , vol.325 , pp. 637-640
    • Lowe, G.1    Meiser, M.2    Berg, H.C.3
  • 5
    • 7744246770 scopus 로고    scopus 로고
    • Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism
    • Samatey F.A., Matsunami H., Imada K., Nagashima S., Shaikh T.R., Thomas D.R., et al. Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism. Nature 431 (2004) 1062-1068
    • (2004) Nature , vol.431 , pp. 1062-1068
    • Samatey, F.A.1    Matsunami, H.2    Imada, K.3    Nagashima, S.4    Shaikh, T.R.5    Thomas, D.R.6
  • 7
    • 0028329280 scopus 로고
    • FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium
    • Ohnishi K., Ohto Y., Aizawa S.-I., Macnab R.M., and Iino T. FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimurium. J. Bacteriol. 176 (1994) 2272-2281
    • (1994) J. Bacteriol. , vol.176 , pp. 2272-2281
    • Ohnishi, K.1    Ohto, Y.2    Aizawa, S.-I.3    Macnab, R.M.4    Iino, T.5
  • 8
    • 33646202330 scopus 로고    scopus 로고
    • The type III flagellar export specificity switch is dependent on FliK ruler and a molecular clock
    • Moriya N., Minamino T., Hughes K.T., Macnab R.M., and Namba K. The type III flagellar export specificity switch is dependent on FliK ruler and a molecular clock. J. Mol. Biol. 359 (2006) 466-477
    • (2006) J. Mol. Biol. , vol.359 , pp. 466-477
    • Moriya, N.1    Minamino, T.2    Hughes, K.T.3    Macnab, R.M.4    Namba, K.5
  • 9
    • 34247585488 scopus 로고    scopus 로고
    • The FliK protein and flagellar hook-length control
    • Waters R.C., O'Toole P.W., and Ryan K.A. The FliK protein and flagellar hook-length control. Protein Sci. 16 (2007) 769-780
    • (2007) Protein Sci. , vol.16 , pp. 769-780
    • Waters, R.C.1    O'Toole, P.W.2    Ryan, K.A.3
  • 11
    • 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
  • 12
    • 0036926615 scopus 로고    scopus 로고
    • A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
    • Stols L., Gu M., Dieckman L., Raffen R., Collart F.R., and Donnelly M.I. A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expression Purif. 25 (2001) 8-15
    • (2001) Protein Expression Purif. , vol.25 , pp. 8-15
    • Stols, L.1    Gu, M.2    Dieckman, L.3    Raffen, R.4    Collart, F.R.5    Donnelly, M.I.6
  • 13
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C., and de Jong P.J. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18 (1990) 6069-6074
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    de Jong, P.J.2
  • 14
    • 0034471444 scopus 로고    scopus 로고
    • A new purification method for overproduced proteins sensitive to endogenous proteases
    • Saijo-Hamano Y., Namba K., and Oosawa K. A new purification method for overproduced proteins sensitive to endogenous proteases. J. Struct. Biol. 132 (2000) 142-146
    • (2000) J. Struct. Biol. , vol.132 , pp. 142-146
    • Saijo-Hamano, Y.1    Namba, K.2    Oosawa, K.3
  • 15
    • 0026737755 scopus 로고
    • Terminal disorder: a common structural feature of the axial proteins of bacterial flagellum?
    • Vonderviszt F., Ishima R., Akasaka K., and Aizawa S.-I. Terminal disorder: a common structural feature of the axial proteins of bacterial flagellum?. J. Mol. Biol. 226 (1992) 575-579
    • (1992) J. Mol. Biol. , vol.226 , pp. 575-579
    • Vonderviszt, F.1    Ishima, R.2    Akasaka, K.3    Aizawa, S.-I.4
  • 16
    • 0024415907 scopus 로고
    • Terminal regions of flagellin are disordered in solution
    • Vonderviszt F., Kanto S., Aizawa S.I., and Namba K. Terminal regions of flagellin are disordered in solution. J. Mol. Biol. 209 (1989) 127-133
    • (1989) J. Mol. Biol. , vol.209 , pp. 127-133
    • Vonderviszt, F.1    Kanto, S.2    Aizawa, S.I.3    Namba, K.4
  • 17
    • 33748997909 scopus 로고    scopus 로고
    • Characterization of the type III export signal of the flagellar hook scaffolding protein FlgD of Escherichia coli
    • Weber-Sparenberg C., Poplau P., Brookman H., Rochon M., Mockel C., Nietschke M., and Jung H. Characterization of the type III export signal of the flagellar hook scaffolding protein FlgD of Escherichia coli. Arch. Microbiol. 186 (2006) 307-316
    • (2006) Arch. Microbiol. , vol.186 , pp. 307-316
    • Weber-Sparenberg, C.1    Poplau, P.2    Brookman, H.3    Rochon, M.4    Mockel, C.5    Nietschke, M.6    Jung, H.7
  • 18
    • 0018420332 scopus 로고
    • Isolation and characterization of bacterial flagellar hook proteins from salmonellae and Escherichia coli
    • Kagawa H., Aizawa S.I., Yamaguchi S., and Ishizu J.I. Isolation and characterization of bacterial flagellar hook proteins from salmonellae and Escherichia coli. J. Bacteriol. 138 (1979) 235-240
    • (1979) J. Bacteriol. , vol.138 , pp. 235-240
    • Kagawa, H.1    Aizawa, S.I.2    Yamaguchi, S.3    Ishizu, J.I.4
  • 19
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. 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
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 20
    • 0027412196 scopus 로고
    • ALSCRIPT: a tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6 (1993) 37-40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 21
    • 24044448971 scopus 로고    scopus 로고
    • Deduction of upstream sequences of Xanthomonas campestris flagellar genes responding to transcription activation by FleQ
    • Hu R.-M., Yang T.-C., Yang S.-H., and Tseng Y.-H. Deduction of upstream sequences of Xanthomonas campestris flagellar genes responding to transcription activation by FleQ. Biochem. Biophys. Res. Commun. 335 (2005) 1035-1043
    • (2005) Biochem. Biophys. Res. Commun. , vol.335 , pp. 1035-1043
    • Hu, R.-M.1    Yang, T.-C.2    Yang, S.-H.3    Tseng, Y.-H.4
  • 22
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 24
    • 33846969140 scopus 로고    scopus 로고
    • Tudor hooks up with DNA repair
    • Corsini L., and Sattler M. Tudor hooks up with DNA repair. Nat. Struct. Biol. 14 (2007) 98-99
    • (2007) Nat. Struct. Biol. , vol.14 , pp. 98-99
    • Corsini, L.1    Sattler, M.2
  • 26
    • 0033559259 scopus 로고    scopus 로고
    • Crystal structure of a heparin- and integrin-binding segment of human fibronectin
    • Sharma A., Askari J.A., Humphries M.J., Jones E.Y., and Stuart D.I. Crystal structure of a heparin- and integrin-binding segment of human fibronectin. EMBO J. 18 (1999) 1468-1479
    • (1999) EMBO J. , vol.18 , pp. 1468-1479
    • Sharma, A.1    Askari, J.A.2    Humphries, M.J.3    Jones, E.Y.4    Stuart, D.I.5
  • 27
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy D.J., Aukhil I., and Erickson H.P. 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84 (1996) 155-164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 29
    • 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
  • 30
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily: domains for cell surface recognition
    • Williams A.F., and Barclay A.N. The immunoglobulin superfamily: domains for cell surface recognition. Annu. Rev. Immunol. 6 (1988) 381-405
    • (1988) Annu. Rev. Immunol. , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 31
    • 0034677663 scopus 로고    scopus 로고
    • The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology
    • Hamill S.J., Steward A., and Clarke J. The folding of an immunoglobulin-like Greek key protein is defined by a common-core nucleus and regions constrained by topology. J. Mol. Biol. 297 (2000) 165-178
    • (2000) J. Mol. Biol. , vol.297 , pp. 165-178
    • Hamill, S.J.1    Steward, A.2    Clarke, J.3
  • 32
    • 36549027487 scopus 로고    scopus 로고
    • Plasticity within the obligatory folding nucleus of an immunoglobulin-like domain
    • Lappalainen I., Hurley M.G., and Clarke J. Plasticity within the obligatory folding nucleus of an immunoglobulin-like domain. J. Mol. Biol. 375 (2008) 547-559
    • (2008) J. Mol. Biol. , vol.375 , pp. 547-559
    • Lappalainen, I.1    Hurley, M.G.2    Clarke, J.3
  • 33
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan M.V., Lee J., Ward I.M., Kim J.-E., Thompson J.R., Chen J.Z., and Mer G. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127 (2006) 1361-1373
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.-E.4    Thompson, J.R.5    Chen, J.Z.6    Mer, G.7
  • 34
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang Y., Fang J., Bedford M.T., Zhang Y., and Xu R.-M. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312 (2006) 748-751
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.-M.5
  • 35
    • 0035876146 scopus 로고    scopus 로고
    • Crystal structure of a heptameric Sm-like protein complex from archaea: implications for the structure and evolution of snRNPs
    • Collins B.M., Harrop S.J., Kornfeld G.D., Dawes I.W., Curmi P.M.G., and Mabbutt B.C. Crystal structure of a heptameric Sm-like protein complex from archaea: implications for the structure and evolution of snRNPs. J. Mol. Biol. 309 (2001) 915-923
    • (2001) J. Mol. Biol. , vol.309 , pp. 915-923
    • Collins, B.M.1    Harrop, S.J.2    Kornfeld, G.D.3    Dawes, I.W.4    Curmi, P.M.G.5    Mabbutt, B.C.6
  • 36
    • 0242380623 scopus 로고    scopus 로고
    • Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli
    • Sauter C., Basquin J., and Suck D. Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli. Nucleic Acids Res. 31 (2003) 4091-4098
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4091-4098
    • Sauter, C.1    Basquin, J.2    Suck, D.3
  • 37
    • 0036645689 scopus 로고    scopus 로고
    • Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein
    • Schumacher M.A., Perarson R.F., Moller T., Valentin-Hansen P., and Brennan R.G. Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J. 21 (2002) 3546-3556
    • (2002) EMBO J. , vol.21 , pp. 3546-3556
    • Schumacher, M.A.1    Perarson, R.F.2    Moller, T.3    Valentin-Hansen, P.4    Brennan, R.G.5
  • 38
    • 0034729584 scopus 로고    scopus 로고
    • RNA degradation: Sm-like proteins wRING the neck of mRNA
    • Pannone B.K., and Wolin S.L. RNA degradation: Sm-like proteins wRING the neck of mRNA. Curr. Biol. 10 (2000) R478-R481
    • (2000) Curr. Biol. , vol.10
    • Pannone, B.K.1    Wolin, S.L.2
  • 39
    • 0028997105 scopus 로고
    • Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs
    • Seraphin B. Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs. EMBO J. 14 (1995) 2089-2098
    • (1995) EMBO J. , vol.14 , pp. 2089-2098
    • Seraphin, B.1
  • 40
    • 0035131438 scopus 로고    scopus 로고
    • Roles of partly unfolded conformations in macromolecular self-assembly
    • Namba K. Roles of partly unfolded conformations in macromolecular self-assembly. Genes Cells 6 (2001) 1-12
    • (2001) Genes Cells , vol.6 , pp. 1-12
    • Namba, K.1
  • 41
    • 0025988180 scopus 로고
    • Role of the disordered terminal regions of flagellin in filament formation and stability
    • Vonderviszt F., Aizawa S.-I., and Namba K. Role of the disordered terminal regions of flagellin in filament formation and stability. J. Mol. Biol. 221 (1991) 1461-1474
    • (1991) J. Mol. Biol. , vol.221 , pp. 1461-1474
    • Vonderviszt, F.1    Aizawa, S.-I.2    Namba, K.3
  • 43
    • 4143100146 scopus 로고    scopus 로고
    • Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins
    • Lundell A., Olin A.I., Morgelin M., al-Karadaghi S., Aspberg A., and Logan D.T. Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins. Structure 12 (2004) 1495-1506
    • (2004) Structure , vol.12 , pp. 1495-1506
    • Lundell, A.1    Olin, A.I.2    Morgelin, M.3    al-Karadaghi, S.4    Aspberg, A.5    Logan, D.T.6
  • 44
    • 0026644395 scopus 로고
    • Proposed acquisition of an animal protein domain by bacteria
    • Bork P., and Doolittle R.F. Proposed acquisition of an animal protein domain by bacteria. Proc. Natl Acad. Sci. USA 89 (1992) 8990-8994
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 8990-8994
    • Bork, P.1    Doolittle, R.F.2
  • 45
    • 0030596502 scopus 로고    scopus 로고
    • Self-assembly of the filament capping protein, FliD, of bacterial flagella into an annular structure
    • Ikeda T., Oosawa K., and Hotani H. Self-assembly of the filament capping protein, FliD, of bacterial flagella into an annular structure. J. Mol. Biol. 259 (1996) 679-686
    • (1996) J. Mol. Biol. , vol.259 , pp. 679-686
    • Ikeda, T.1    Oosawa, K.2    Hotani, H.3
  • 47
    • 0028058957 scopus 로고
    • Nucleotide sequence of the flgD gene of Salmonella typhimurium which is essential for flagellar hook formation
    • Kutsukake K., and Doi H. Nucleotide sequence of the flgD gene of Salmonella typhimurium which is essential for flagellar hook formation. Biochim. Biophys. Acta 1218 (1994) 443-446
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 443-446
    • Kutsukake, K.1    Doi, H.2
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of the X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of the X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.