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Volumn 62, Issue 2, 2006, Pages 322-328

Crystal structure of ScpB from Chlorobium tepidum, a protein involved in chromosome partitioning

Author keywords

Chlorobium tepidum; Chromosome partitioning; Crystal structure

Indexed keywords

BACTERIAL PROTEIN; DNA BINDING PROTEIN; HELIX LOOP HELIX PROTEIN; MONOMER; SCPA PROTEIN; SCPB PROTEIN; UNCLASSIFIED DRUG;

EID: 30144435867     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20751     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 0032901198 scopus 로고    scopus 로고
    • SMC-mediated chromosome mechanics: A conserved scheme from bacteria to vertebrates?
    • Hirano T. SMC-mediated chromosome mechanics: a conserved scheme from bacteria to vertebrates? Genes Dev 1999;13:11-19.
    • (1999) Genes Dev , vol.13 , pp. 11-19
    • Hirano, T.1
  • 2
    • 0033167929 scopus 로고    scopus 로고
    • Structural maintenance of chromosomes (SMC) proteins: Conserved molecular properties for multiple biological functions
    • Strunnikov AV, Jessberger R. Structural maintenance of chromosomes (SMC) proteins: conserved molecular properties for multiple biological functions. Eur J Biochem 1999;263:6-13.
    • (1999) Eur J Biochem , vol.263 , pp. 6-13
    • Strunnikov, A.V.1    Jessberger, R.2
  • 3
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner KP, Karcher A, Shin DS, Craig L, Arthur LM, Carney JP, Tainer JA. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 2000;101:789-800.
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 4
    • 0035830484 scopus 로고    scopus 로고
    • Crystal structure of the Smc head domain: An ABC ATPase with 900 residues antiparallel coiled-coil inserted
    • Lowe J, Cordell SC, Van Den Ent F. Crystal structure of the Smc head domain: an ABC ATPase with 900 residues antiparallel coiled-coil inserted. J Mol Biol 2001;306:25-35.
    • (2001) J Mol Biol , vol.306 , pp. 25-35
    • Lowe, J.1    Cordell, S.C.2    Van Den Ent, F.3
  • 5
    • 0036177230 scopus 로고    scopus 로고
    • Structural maintenance of chromosomes (SMC) proteins, a family of conserved ATPases
    • REVIEWS3003
    • Harvey SH, Krien MJ, O'Connell MJ. Structural maintenance of chromosomes (SMC) proteins, a family of conserved ATPases. Genome Biol 2003;3:REVIEWS3003.
    • (2003) Genome Biol , vol.3
    • Harvey, S.H.1    Krien, M.J.2    O'Connell, M.J.3
  • 6
    • 0042132009 scopus 로고    scopus 로고
    • A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure
    • Volkov A, Mascarenhas J, Andrei-Selmer C, Ulrich HD, Graumann PL. A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure. Mol Cell Biol 2003;23: 5638-5650.
    • (2003) Mol Cell Biol , vol.23 , pp. 5638-5650
    • Volkov, A.1    Mascarenhas, J.2    Andrei-Selmer, C.3    Ulrich, H.D.4    Graumann, P.L.5
  • 7
    • 0026069582 scopus 로고
    • The new gen MukB codes for a 177kD protein with coiled-coil domains involved in chromosome partitioning of Escherichia coli
    • Niki H, Jaffe A, Imamura R, Ogura T, Hiraga S. The new gen MukB codes for a 177kD protein with coiled-coil domains involved in chromosome partitioning of Escherichia coli. EMBO J 1991;10: 183-193.
    • (1991) EMBO J , vol.10 , pp. 183-193
    • Niki, H.1    Jaffe, A.2    Imamura, R.3    Ogura, T.4    Hiraga, S.5
  • 8
    • 0033569886 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of Mukb: A protein involved in chromosome partitioning
    • Van Den Ent F, Lockhart A, Kendrick-Jones J, Lowe J. Crystal structure of the N-terminal domain of Mukb: a protein involved in chromosome partitioning. Struct Fold Des 1999;7: 1181-1187.
    • (1999) Struct Fold des , vol.7 , pp. 1181-1187
    • Van Den Ent, F.1    Lockhart, A.2    Kendrick-Jones, J.3    Lowe, J.4
  • 9
    • 0036049587 scopus 로고    scopus 로고
    • Discovery of two novel families of proteins that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB
    • Soppa J, Kobayashi K, Noirot-Gros MF, Oesterhelt D, Ehrlich SD, Dervyn E, Ogasawara N, Moriya S. Discovery of two novel families of proteins -that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB. Mol Microbiol 2002;45: 59-71.
    • (2002) Mol Microbiol , vol.45 , pp. 59-71
    • Soppa, J.1    Kobayashi, K.2    Noirot-Gros, M.F.3    Oesterhelt, D.4    Ehrlich, S.D.5    Dervyn, E.6    Ogasawara, N.7    Moriya, S.8
  • 10
    • 0036434993 scopus 로고    scopus 로고
    • Subcellular localization of the Bacillus subtilis structural maintenance of chromosomes (SMC) protein
    • Lindow JC, Kuwano M, Moriya S, Grossman AD. Subcellular localization of the Bacillus subtilis structural maintenance of chromosomes (SMC) protein. Mol Microbiol 2002;46:997-1009.
    • (2002) Mol Microbiol , vol.46 , pp. 997-1009
    • Lindow, J.C.1    Kuwano, M.2    Moriya, S.3    Grossman, A.D.4
  • 11
    • 0037124369 scopus 로고    scopus 로고
    • Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein
    • Mascarenhas J, Soppa J, Strunnikov AV, Graumann, PL. Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein. EMBO J 2002;17:3108-3118.
    • (2002) EMBO J , vol.17 , pp. 3108-3118
    • Mascarenhas, J.1    Soppa, J.2    Strunnikov, A.V.3    Graumann, P.L.4
  • 13
    • 0036242551 scopus 로고    scopus 로고
    • Molecular architecture of SMC proteins and the yeast cohesin complex
    • Haering C, Löwe J, Hochwagen A, Nasmyth K. Molecular architecture of SMC proteins and the yeast cohesin complex. Mol Cell 2002;9:773-788.
    • (2002) Mol Cell , vol.9 , pp. 773-788
    • Haering, C.1    Löwe, J.2    Hochwagen, A.3    Nasmyth, K.4
  • 14
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. Protein structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 15
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis C, de Jong PJ. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 1990;20:6069-6074.
    • (1990) Nucleic Acids Res , vol.20 , pp. 6069-6074
    • Aslanidis, C.1    De Jong, P.J.2
  • 17
    • 16644371341 scopus 로고    scopus 로고
    • Optimum solubility (OS) screening: An efficient method to optimize buffer conditions for homogeneity and crystallization of proteins
    • Jancarik J, Pufan R, Hong C, Kim R, Kim SH. Optimum solubility (OS) screening: an efficient method to optimize buffer conditions for homogeneity and crystallization of proteins. Acta Crystallogr D 2004;60:1670-1673.
    • (2004) Acta Crystallogr D , vol.60 , pp. 1670-1673
    • Jancarik, J.1    Pufan, R.2    Hong, C.3    Kim, R.4    Kim, S.H.5
  • 18
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik J, Kim SH. Sparse matrix sampling: a screening method for crystallization of proteins. J Appl Crystallogr 1991;24:409-411.
    • (1991) J Appl Crystallogr , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.H.2
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Procession of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Procession of x-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 21
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: Recent developments in and around SHARP 2.0
    • Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr D Biol Crystallogr 2003;59:2023-2030.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou ZY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-117.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-117
    • Jones, T.A.1    Zou, Z.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MD, Isupov MN, Murshudov GN. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr D Biol Crystallogr 2001;57:122-133.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 25
    • 0000243829 scopus 로고
    • PRO-CHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R, MacArthur M, Hutchinson E, Thorton J. PRO-CHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Hutchinson, E.3    Thorton, J.4
  • 27
    • 0033546005 scopus 로고    scopus 로고
    • Crystal structure of the Z domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA
    • Schwartz T, Rould MA, Lowenhaupt K, Herbert A, Rich A. Crystal structure of the Z domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA. Science 1999;284:1841-1845.
    • (1999) Science , vol.284 , pp. 1841-1845
    • Schwartz, T.1    Rould, M.A.2    Lowenhaupt, K.3    Herbert, A.4    Rich, A.5
  • 28
    • 3343008805 scopus 로고    scopus 로고
    • Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins
    • Hirano M, Hirano T. Positive and negative regulation of SMC-DNA interactions by ATP and accessory proteins. EMBO J 2004;23:2664-2673.
    • (2004) EMBO J , vol.23 , pp. 2664-2673
    • Hirano, M.1    Hirano, T.2
  • 30
    • 0026244229 scopus 로고
    • A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 1991;24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0000732609 scopus 로고
    • GRASP-graphical representation and analysis of surface properties
    • Nicholls A, Bharadwaj R, Honig B. GRASP-graphical representation and analysis of surface properties. Biophys J 1993;64: A166.
    • (1993) Biophys J , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


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