메뉴 건너뛰기




Volumn 185, Issue 14, 2003, Pages 4066-4073

Crystal structure of the hyperthermophilic archaeal DNA-binding protein Sso10b2 at a resolution of 1.85 Angstroms

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL PROTEIN; BACTERIAL PROTEIN; DEOXYRIBONUCLEASE I; DIMER; DNA BINDING PROTEIN; PROTEIN SSO10B2; RNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 0037478787     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.14.4066-4073.2003     Document Type: Article
Times cited : (56)

References (30)
  • 1
    • 0037023326 scopus 로고    scopus 로고
    • The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation
    • Bell, S. D., C. H. Botting, B. N. Wardleworth, S. P. Jackson, and M. F. White. 2002. The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation. Science 296:148-151.
    • (2002) Science , vol.296 , pp. 148-151
    • Bell, S.D.1    Botting, C.H.2    Wardleworth, B.N.3    Jackson, S.P.4    White, M.F.5
  • 2
    • 0029111710 scopus 로고
    • X-ray crystallography shows that translational initiation factor 1F3 consists of two compact α/β domains linked by an α-helix
    • Biou, V., F. Shu, and V. Ramakrishnan. 1995. X-ray crystallography shows that translational initiation factor 1F3 consists of two compact α/β domains linked by an α-helix. EMBO J. 14:4056-4064.
    • (1995) EMBO J. , vol.14 , pp. 4056-4064
    • Biou, V.1    Shu, F.2    Ramakrishnan, V.3
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50:760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 5
    • 0032060976 scopus 로고    scopus 로고
    • A role for zinc in the regulation of gene expression
    • Cousins, R. J. 1998. A role for zinc in the regulation of gene expression. Proc. Nutr. Soc. 57:307-311.
    • (1998) Proc. Nutr. Soc. , vol.57 , pp. 307-311
    • Cousins, R.J.1
  • 6
    • 0026690143 scopus 로고
    • Structure-function analysis of Escherichia coli translation initiation factor IF3: Tyrosine 107 and lysine 110 are required for ribosome binding
    • De Bellis, D., D. Liveris, D. Goss, S. Ringquist, and I. Schwartz. 1992. Structure-function analysis of Escherichia coli translation initiation factor IF3: tyrosine 107 and lysine 110 are required for ribosome binding. Biochemistry 31:11984-11990.
    • (1992) Biochemistry , vol.31 , pp. 11984-11990
    • De Bellis, D.1    Liveris, D.2    Goss, D.3    Ringquist, S.4    Schwartz, I.5
  • 7
    • 0034986024 scopus 로고    scopus 로고
    • DNA-binding proteins Sac7d and Sso7d from Sulfolobus
    • Edmondson, S. P., and J. W. Shriver. 2001. DNA-binding proteins Sac7d and Sso7d from Sulfolobus. Methods Enzymol. 334:129-145.
    • (2001) Methods Enzymol. , vol.334 , pp. 129-145
    • Edmondson, S.P.1    Shriver, J.W.2
  • 8
    • 0032961053 scopus 로고    scopus 로고
    • Identification of the gene encoding archaeal-specific DNA-binding proteins of the Sac10b family
    • Forterre, P., F. Confalonieri, and S. Knapp. 1999. Identification of the gene encoding archaeal-specific DNA-binding proteins of the Sac10b family. Mol. Microbiol. 32:669-670.
    • (1999) Mol. Microbiol. , vol.32 , pp. 669-670
    • Forterre, P.1    Confalonieri, F.2    Knapp, S.3
  • 10
    • 0022478821 scopus 로고
    • Ribosomal and DNA binding proteins of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • Grote, M., J. Dijk, and R. Reinhardt. 1986. Ribosomal and DNA binding proteins of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biochim. Biophys. Acta 873:405-413.
    • (1986) Biochim. Biophys. Acta , vol.873 , pp. 405-413
    • Grote, M.1    Dijk, J.2    Reinhardt, R.3
  • 11
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm, L., and C. Sander. 1998. Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 26:316-319.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 12
    • 0034711380 scopus 로고    scopus 로고
    • High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division
    • Katoh, E., T. Hatta, H Shindo, Y. Ishii, H. Yamada, T. Mizuno, and T. Yamazaki. 2000. High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division. J. Mol. Biol. 304:219-229.
    • (2000) J. Mol. Biol. , vol.304 , pp. 219-229
    • Katoh, E.1    Hatta, T.2    Shindo, H.3    Ishii, Y.4    Yamada, H.5    Mizuno, T.6    Yamazaki, T.7
  • 13
    • 0021764377 scopus 로고
    • The amino acid sequence of a small DNA binding protein from the archaeabacterium Sulfolobus solfataricus
    • Kimura, M., J. Kimura, P. Davie, R. Reinhardt, and J. Dijk. 1984. The amino acid sequence of a small DNA binding protein from the archaeabacterium Sulfolobus solfataricus. FEBS Lett. 176:176-178.
    • (1984) FEBS Lett. , vol.176 , pp. 176-178
    • Kimura, M.1    Kimura, J.2    Davie, P.3    Reinhardt, R.4    Dijk, J.5
  • 14
    • 0030596013 scopus 로고    scopus 로고
    • Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus
    • Knapp, S., A. Karshikoff, K. D. Berndt, P. Christova, B. Atanasov, and R. Ladenstein. 1996. Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus. J. Mol. Biol. 264:1132-1144.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1132-1144
    • Knapp, S.1    Karshikoff, A.2    Berndt, K.D.3    Christova, P.4    Atanasov, B.5    Ladenstein, R.6
  • 15
    • 0001270373 scopus 로고
    • Electron microscopic study of DNA complexes with proteins from the Archaebacterium Sulfolobus acidocaldarius
    • Lurz, R., M. Grote, J. Dijk, R. Reinhardt, and B. Dobrinski. 1986. Electron microscopic study of DNA complexes with proteins from the Archaebacterium Sulfolobus acidocaldarius. EMBO J. 5:3715-3721.
    • (1986) EMBO J. , vol.5 , pp. 3715-3721
    • Lurz, R.1    Grote, M.2    Dijk, J.3    Reinhardt, R.4    Dobrinski, B.5
  • 16
    • 0031957673 scopus 로고    scopus 로고
    • Small abundant DNA binding proteins from the thermoacidophilic archaeon Sulfolobus shibatae constrain negative DNA supercoils
    • Mai, V. Q., X. Chen, R. Hong, and L. Huang. 1998. Small abundant DNA binding proteins from the thermoacidophilic archaeon Sulfolobus shibatae constrain negative DNA supercoils. J. Bacteriol. 180:2560-2563.
    • (1998) J. Bacteriol. , vol.180 , pp. 2560-2563
    • Mai, V.Q.1    Chen, X.2    Hong, R.3    Huang, L.4
  • 17
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. 1999. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125:156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 18
    • 0019473006 scopus 로고
    • Structure-function relationship in Escherichia coli initiation factors
    • Ohsawa, H., and C. Gualerzi. 1981. Structure-function relationship in Escherichia coli initiation factors. J. Biol. Chem. 256:4905-4912.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4905-4912
    • Ohsawa, H.1    Gualerzi, C.2
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of the X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of the 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
  • 22
    • 0023818825 scopus 로고
    • Structure refined to 2 Å of a nicked DNA octanucleotide complex with DNase I
    • Suck, D., A. Lahm, and C. Oefner. 1988. Structure refined to 2 Å of a nicked DNA octanucleotide complex with DNase I. Nature 332:464-468.
    • (1988) Nature , vol.332 , pp. 464-468
    • Suck, D.1    Lahm, A.2    Oefner, C.3
  • 23
  • 24
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C., and J. Berendzen, 1999. Automated MAD and MIR structure solution. Acta Crystallogr. D55:849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 25
    • 0037009516 scopus 로고    scopus 로고
    • Structure of Alba: An archaeal chromatin protein modulated by acetylation
    • Wardleworth, B. N., R. J. Russell, S. D. Bell, G. L. Taylor, and M. F. White. 2002. Structure of Alba: an archaeal chromatin protein modulated by acetylation. EMBO J. 21:4654-4662.
    • (2002) EMBO J. , vol.21 , pp. 4654-4662
    • Wardleworth, B.N.1    Russell, R.J.2    Bell, S.D.3    Taylor, G.L.4    White, M.F.5
  • 26
    • 0035214721 scopus 로고    scopus 로고
    • Preliminary crystallographic studies of the double-stranded DNA binding protein Sso10b from Sulfolobus solfataricus
    • Wardleworth, B. N., R. Russell, M. F. White, and G. L. Taylor. 2001. Preliminary crystallographic studies of the double-stranded DNA binding protein Sso10b from Sulfolobus solfataricus. Acta Crystallogr. D57:1893-1894.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1893-1894
    • Wardleworth, B.N.1    Russell, R.2    White, M.F.3    Taylor, G.L.4
  • 27
    • 0032419957 scopus 로고    scopus 로고
    • RNA recognition by arginine-rich peptide motifs
    • Weiss, M. A., and N. Narayana. 1999. RNA recognition by arginine-rich peptide motifs. Biopolymers 48:167-180.
    • (1999) Biopolymers , vol.48 , pp. 167-180
    • Weiss, M.A.1    Narayana, N.2
  • 29
    • 0033917479 scopus 로고    scopus 로고
    • An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion
    • Xue, H., R. Guo, Y. Wen, D. Liu, and L. Huang. 2000. An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion. J. Bacteriol. 182:3929-3933.
    • (2000) J. Bacteriol. , vol.182 , pp. 3929-3933
    • Xue, H.1    Guo, R.2    Wen, Y.3    Liu, D.4    Huang, L.5
  • 30
    • 0031948461 scopus 로고    scopus 로고
    • The YhhP gene encoding a small ubiquitous protein is fundamental for normal cell growth of Escherichia coli
    • Yamashino, T., M. Isomura, C. Ueguchi, and T. Mizuno. 1998. The YhhP gene encoding a small ubiquitous protein is fundamental for normal cell growth of Escherichia coli. J. Bacteriol. 180:2257-2261.
    • (1998) J. Bacteriol. , vol.180 , pp. 2257-2261
    • Yamashino, T.1    Isomura, M.2    Ueguchi, C.3    Mizuno, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.