메뉴 건너뛰기




Volumn 372, Issue 5, 2007, Pages 1293-1304

The Putative DNA-Binding Protein Sto12a from the Thermoacidophilic Archaeon Sulfolobus tokodaii Contains Intrachain and Interchain Disulfide Bonds

Author keywords

disulfide bond; DNA binding protein; Sulfolobus tokodaii; thermophile; winged helix turn helix domain

Indexed keywords

DNA BINDING PROTEIN; HOMODIMER; SELENOMETHIONINE; WINGED HELIX TRANSCRIPTION FACTOR;

EID: 34548507202     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.07.051     Document Type: Article
Times cited : (8)

References (57)
  • 1
    • 0035980098 scopus 로고    scopus 로고
    • Complete genome sequence of an aerobic thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7
    • Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M., et al. Complete genome sequence of an aerobic thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7. DNA Res. 8 (2001) 123-140
    • (2001) DNA Res. , vol.8 , pp. 123-140
    • Kawarabayasi, Y.1    Hino, Y.2    Horikawa, H.3    Jin-no, K.4    Takahashi, M.5    Sekine, M.6
  • 3
    • 21844477811 scopus 로고    scopus 로고
    • The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota
    • Chen L., Brugger K., Skovgaard M., Redder P., She Q., Torarinsson E., et al. The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota. J. Bacteriol. 187 (2005) 4992-4999
    • (2005) J. Bacteriol. , vol.187 , pp. 4992-4999
    • Chen, L.1    Brugger, K.2    Skovgaard, M.3    Redder, P.4    She, Q.5    Torarinsson, E.6
  • 5
    • 1042302417 scopus 로고    scopus 로고
    • Structure and function of the feast/famine regulatory proteins, FFRPs
    • Suzuki M. Structure and function of the feast/famine regulatory proteins, FFRPs. Proc. Jpn. Acad. Ser. B 79 (2003) 274-289
    • (2003) Proc. Jpn. Acad. Ser. B , vol.79 , pp. 274-289
    • Suzuki, M.1
  • 6
    • 0032985667 scopus 로고    scopus 로고
    • An Lrp-like protein of the hyperthermophilic archaeon Sulfolobus solfataricus which binds to its own promoter
    • Napoli A., van der Oost J., Sensen C.W., Charlebois R.L., Rossi M., and Ciaramella M. An Lrp-like protein of the hyperthermophilic archaeon Sulfolobus solfataricus which binds to its own promoter. J. Bacteriol. 181 (1999) 1474-1480
    • (1999) J. Bacteriol. , vol.181 , pp. 1474-1480
    • Napoli, A.1    van der Oost, J.2    Sensen, C.W.3    Charlebois, R.L.4    Rossi, M.5    Ciaramella, M.6
  • 7
    • 0036034720 scopus 로고    scopus 로고
    • High resolution contact probing of the Lrp-like DNA-binding protein Ss-Lrp from the hyperthermoacidophilic crenarchaeote Sulfolobus solfataricus P2
    • Enoru-Eta J., Gigot D., Glansdorff N., and Charlier D. High resolution contact probing of the Lrp-like DNA-binding protein Ss-Lrp from the hyperthermoacidophilic crenarchaeote Sulfolobus solfataricus P2. Mol. Microbiol. 45 (2002) 1541-1555
    • (2002) Mol. Microbiol. , vol.45 , pp. 1541-1555
    • Enoru-Eta, J.1    Gigot, D.2    Glansdorff, N.3    Charlier, D.4
  • 8
    • 6344272907 scopus 로고    scopus 로고
    • Ss-LrpB, a novel Lrp-like regulator of Sulfolobus solfataricus P2, binds cooperatively to three conserved targets in its own control region
    • Peeters E., Thia-Toong T.L., Gigot D., Maes D., and Charlier D. Ss-LrpB, a novel Lrp-like regulator of Sulfolobus solfataricus P2, binds cooperatively to three conserved targets in its own control region. Mol. Microbiol. 54 (2004) 321-336
    • (2004) Mol. Microbiol. , vol.54 , pp. 321-336
    • Peeters, E.1    Thia-Toong, T.L.2    Gigot, D.3    Maes, D.4    Charlier, D.5
  • 9
    • 0034044849 scopus 로고    scopus 로고
    • Purification and characterization of Sa-Lrp, a DNA-binding protein from the extreme thermoacidophilic archaeon Sulfolobus acidocaldarius homologous to the bacterial global transcriptional regulator Lrp
    • Enoru-Eta J., Gigot D., Thia-Toong T.L., Glansdorff N., and Charlier D. Purification and characterization of Sa-Lrp, a DNA-binding protein from the extreme thermoacidophilic archaeon Sulfolobus acidocaldarius homologous to the bacterial global transcriptional regulator Lrp. J. Bacteriol. 182 (2000) 3661-3672
    • (2000) J. Bacteriol. , vol.182 , pp. 3661-3672
    • Enoru-Eta, J.1    Gigot, D.2    Thia-Toong, T.L.3    Glansdorff, N.4    Charlier, D.5
  • 10
    • 0037119358 scopus 로고    scopus 로고
    • The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability
    • Brinkman A.B., Bell S.D., Lebbink R.J., de Vos W. M., and van der Oost J. The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability. J. Biol. Chem. 277 (2002) 29537-29549
    • (2002) J. Biol. Chem. , vol.277 , pp. 29537-29549
    • Brinkman, A.B.1    Bell, S.D.2    Lebbink, R.J.3    de Vos, W. M.4    van der Oost, J.5
  • 12
    • 0036890204 scopus 로고    scopus 로고
    • Holding it together: chromatin in the Archaea
    • White M.F., and Bell S.D. Holding it together: chromatin in the Archaea. Trends Genet. 18 (2002) 621-626
    • (2002) Trends Genet. , vol.18 , pp. 621-626
    • White, M.F.1    Bell, S.D.2
  • 13
    • 0038575389 scopus 로고    scopus 로고
    • Archaeal chromatin and transcription
    • Reeve J.N. Archaeal chromatin and transcription. Mol. Microbiol. 48 (2003) 587-598
    • (2003) Mol. Microbiol. , vol.48 , pp. 587-598
    • Reeve, J.N.1
  • 14
    • 4143109111 scopus 로고    scopus 로고
    • The hyperthermophile protein Sso10a is a dimer of winged helix DNA-binding domains linked by an antiparallel coiled coil rod
    • Chen L., Chen L.R., Zhou X.E., Wang Y., Kahsai M. A., Clark A.T., et al. The hyperthermophile protein Sso10a is a dimer of winged helix DNA-binding domains linked by an antiparallel coiled coil rod. J. Mol. Biol. 341 (2004) 73-91
    • (2004) J. Mol. Biol. , vol.341 , pp. 73-91
    • Chen, L.1    Chen, L.R.2    Zhou, X.E.3    Wang, Y.4    Kahsai, M. A.5    Clark, A.T.6
  • 15
    • 14344265435 scopus 로고    scopus 로고
    • Solution structure, stability, and flexibility of Sso10a: a hyperthermophile coiled-coil DNA-binding protein
    • Kahsai M.A., Vogler B., Clark A.T., Edmondson S. P., and Shriver J.W. Solution structure, stability, and flexibility of Sso10a: a hyperthermophile coiled-coil DNA-binding protein. Biochemistry 44 (2005) 2822-2832
    • (2005) Biochemistry , vol.44 , pp. 2822-2832
    • Kahsai, M.A.1    Vogler, B.2    Clark, A.T.3    Edmondson, S. P.4    Shriver, J.W.5
  • 16
    • 27844543263 scopus 로고    scopus 로고
    • Archaeal chromatin proteins: different structures but common function?
    • Sandman K., and Reeve J.N. Archaeal chromatin proteins: different structures but common function?. Curr. Opin. Microbiol. 8 (2005) 656-661
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 656-661
    • Sandman, K.1    Reeve, J.N.2
  • 17
    • 0037096967 scopus 로고    scopus 로고
    • DNA bending, compaction and negative supercoiling by the architectural protein Sso7d of Sulfolobus solfataricus
    • Napoli A., Zivanovic Y., Bocs C., Buhler C., Rossi M., Forterre P., and Ciaramella M. DNA bending, compaction and negative supercoiling by the architectural protein Sso7d of Sulfolobus solfataricus. Nucleic Acids Res. 30 (2002) 2656-2662
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2656-2662
    • Napoli, A.1    Zivanovic, Y.2    Bocs, C.3    Buhler, C.4    Rossi, M.5    Forterre, P.6    Ciaramella, M.7
  • 18
    • 33750947874 scopus 로고    scopus 로고
    • Photoreactivation of DNA by an archaeal nucleoprotein Sso7d
    • Tashiro R., Wang A.H., and Sugiyama H. Photoreactivation of DNA by an archaeal nucleoprotein Sso7d. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 16655-16659
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16655-16659
    • Tashiro, R.1    Wang, A.H.2    Sugiyama, H.3
  • 19
    • 0034644686 scopus 로고    scopus 로고
    • The chromosomal protein Sso7d of the crenarchaeon Sulfolobus solfataricus rescues aggregated proteins in an ATP hydrolysis-dependent manner
    • Guagliardi A., Cerchia L., Moracci M., and Rossi M. The chromosomal protein Sso7d of the crenarchaeon Sulfolobus solfataricus rescues aggregated proteins in an ATP hydrolysis-dependent manner. J. Biol. Chem. 275 (2000) 31813-33188
    • (2000) J. Biol. Chem. , vol.275 , pp. 31813-33188
    • Guagliardi, A.1    Cerchia, L.2    Moracci, M.3    Rossi, M.4
  • 20
    • 3142767444 scopus 로고    scopus 로고
    • Reversion of protein aggregation mediated by Sso7d in cell extracts of Sulfolobus solfataricus
    • Guagliardi A., Mancusi L., and Rossi M. Reversion of protein aggregation mediated by Sso7d in cell extracts of Sulfolobus solfataricus. Biochem. J. 381 (2004) 249-255
    • (2004) Biochem. J. , vol.381 , pp. 249-255
    • Guagliardi, A.1    Mancusi, L.2    Rossi, M.3
  • 21
    • 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., Guo R., Wen Y., Liu D., and Huang L. An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion. J. Bacteriol. 182 (2000) 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
  • 22
    • 0035815657 scopus 로고    scopus 로고
    • A novel member of the bacterial-archaeal regulator family is a nonspecific DNA-binding protein and induces positive supercoiling
    • Napoli A., Kvaratskelia M., White M.F., Rossi M., and Ciaramella M. A novel member of the bacterial-archaeal regulator family is a nonspecific DNA-binding protein and induces positive supercoiling. J. Biol. Chem. 276 (2001) 10745-10752
    • (2001) J. Biol. Chem. , vol.276 , pp. 10745-10752
    • Napoli, A.1    Kvaratskelia, M.2    White, M.F.3    Rossi, M.4    Ciaramella, M.5
  • 24
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm L., and Sander C. Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 26 (1998) 316-319
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 25
    • 0033546005 scopus 로고    scopus 로고
    • Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA
    • Schwartz T., Rould M.A., Lowenhaupt K., Herbert A., and Rich A. Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA. Science 284 (1999) 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
  • 26
    • 0037162464 scopus 로고    scopus 로고
    • Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds
    • Mallick P., Boutz D.R., Eisenberg D., and Yeates T.O. Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 9679-9684
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9679-9684
    • Mallick, P.1    Boutz, D.R.2    Eisenberg, D.3    Yeates, T.O.4
  • 27
    • 0029798075 scopus 로고    scopus 로고
    • Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus
    • Jiang Y., Nock S., Nesper M., Sprinzl M., and Sigler P. B. Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus. Biochemistry 35 (1996) 10269-10278
    • (1996) Biochemistry , vol.35 , pp. 10269-10278
    • Jiang, Y.1    Nock, S.2    Nesper, M.3    Sprinzl, M.4    Sigler, P. B.5
  • 28
    • 0034636987 scopus 로고    scopus 로고
    • The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds
    • Toth E.A., Worby C., Dixon J.E., Goedken E.R., Marqusee S., and Yeates T.O. The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. J. Mol. Biol. 301 (2000) 433-450
    • (2000) J. Mol. Biol. , vol.301 , pp. 433-450
    • Toth, E.A.1    Worby, C.2    Dixon, J.E.3    Goedken, E.R.4    Marqusee, S.5    Yeates, T.O.6
  • 29
    • 0037022796 scopus 로고    scopus 로고
    • A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond
    • Meyer J., Clay M.D., Johnson M.K., Stubna A., Munck E., Higgins C., and Wittung-Stafshede P. A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond. Biochemistry 41 (2002) 3096-3108
    • (2002) Biochemistry , vol.41 , pp. 3096-3108
    • Meyer, J.1    Clay, M.D.2    Johnson, M.K.3    Stubna, A.4    Munck, E.5    Higgins, C.6    Wittung-Stafshede, P.7
  • 30
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz W.A., Aslund F., Holmgren A., and Beckwith J. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272 (1997) 15661-15667
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 31
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob U., Muse W., Eser M., and Bardwell J.C. Chaperone activity with a redox switch. Cell 96 (1999) 341-352
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 32
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M., Aslund F., and Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279 (1998) 1718-1721
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 33
    • 0027270989 scopus 로고
    • Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
    • Clark K.L., Halay E.D., Lai E., and Burley S.K. Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5. Nature 364 (1993) 412-420
    • (1993) Nature , vol.364 , pp. 412-420
    • Clark, K.L.1    Halay, E.D.2    Lai, E.3    Burley, S.K.4
  • 34
    • 0033019592 scopus 로고    scopus 로고
    • Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex
    • Jin C., Marsden I., Chen X., and Liao X. Dynamic DNA contacts observed in the NMR structure of winged helix protein-DNA complex. J. Mol. Biol. 289 (1999) 683-690
    • (1999) J. Mol. Biol. , vol.289 , pp. 683-690
    • Jin, C.1    Marsden, I.2    Chen, X.3    Liao, X.4
  • 35
    • 0035170973 scopus 로고    scopus 로고
    • The Mu repressor-DNA complex contains an immobilized 'wing' within the minor groove
    • Wojciak J.M., Iwahara J., and Clubb R.T. The Mu repressor-DNA complex contains an immobilized 'wing' within the minor groove. Nat. Struct. Biol. 8 (2001) 84-90
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 84-90
    • Wojciak, J.M.1    Iwahara, J.2    Clubb, R.T.3
  • 37
    • 0033559680 scopus 로고    scopus 로고
    • The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds
    • Hall D.R., Gourley D.G., Leonard G.A., Duke E. M., Anderson L.A., Boxer D.H., and Hunter W.N. The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds. EMBO J. 18 (1999) 1435-1446
    • (1999) EMBO J. , vol.18 , pp. 1435-1446
    • Hall, D.R.1    Gourley, D.G.2    Leonard, G.A.3    Duke, E. M.4    Anderson, L.A.5    Boxer, D.H.6    Hunter, W.N.7
  • 38
    • 0035861738 scopus 로고    scopus 로고
    • Crystal structure of MtaN, a global multidrug transporter gene activator
    • Godsey M.H., Baranova N.N., Neyfakh A.A., and Brennan R.G. Crystal structure of MtaN, a global multidrug transporter gene activator. J. Biol. Chem. 276 (2001) 47178-47184
    • (2001) J. Biol. Chem. , vol.276 , pp. 47178-47184
    • Godsey, M.H.1    Baranova, N.N.2    Neyfakh, A.A.3    Brennan, R.G.4
  • 39
    • 0028918469 scopus 로고
    • Crystal structure of the replication terminator protein from B. subtilis at 2.6 Å
    • Bussiere D.E., Bastia D., and White S.W. Crystal structure of the replication terminator protein from B. subtilis at 2.6 Å. Cell 80 (1995) 651-660
    • (1995) Cell , vol.80 , pp. 651-660
    • Bussiere, D.E.1    Bastia, D.2    White, S.W.3
  • 40
    • 0000920828 scopus 로고
    • The packing of alpha-helices: simple coiled coils
    • Crick F.H.C. The packing of alpha-helices: simple coiled coils. Acta Crystallogr. 6 (1953) 689-697
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 41
    • 0035853291 scopus 로고    scopus 로고
    • Socket: a program for identifying and analysing coiled-coil motifs within protein structures
    • Walshaw J., and Woolfson D.N. Socket: a program for identifying and analysing coiled-coil motifs within protein structures. J. Mol. Biol. 307 (2001) 1427-1450
    • (2001) J. Mol. Biol. , vol.307 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2
  • 43
    • 0025366034 scopus 로고
    • Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity
    • Kuramitsu S., Hiromi K., Hayashi H., Morino Y., and Kagamiyama H. Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity. Biochemistry 29 (1990) 5469-5476
    • (1990) Biochemistry , vol.29 , pp. 5469-5476
    • Kuramitsu, S.1    Hiromi, K.2    Hayashi, H.3    Morino, Y.4    Kagamiyama, H.5
  • 44
  • 45
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of 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
  • 46
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 49
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 51
  • 52
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 53
    • 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
  • 54
    • 0037166263 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima 0065, a member of the IclR transcriptional factor family
    • Zhang R.G., Kim Y., Skarina T., Beasley S., Laskowski R., Arrowsmith C., et al. Crystal structure of Thermotoga maritima 0065, a member of the IclR transcriptional factor family. J. Biol. Chem. 277 (2002) 9183-19190
    • (2002) J. Biol. Chem. , vol.277 , pp. 9183-19190
    • Zhang, R.G.1    Kim, Y.2    Skarina, T.3    Beasley, S.4    Laskowski, R.5    Arrowsmith, C.6
  • 55
    • 0032536158 scopus 로고    scopus 로고
    • Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins
    • Cook W.J., Kar S.R., Taylor K.B., and Hall L.M. Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J. Mol. Biol. 275 (1998) 337-346
    • (1998) J. Mol. Biol. , vol.275 , pp. 337-346
    • Cook, W.J.1    Kar, S.R.2    Taylor, K.B.3    Hall, L.M.4
  • 56
    • 14244256059 scopus 로고    scopus 로고
    • Crystal structures of the BlaI repressor from Staphylococcus aureus and its complex with DNA: insights into transcriptional regulation of the bla and mec operons
    • Safo M.K., Zhao Q., Ko T.P., Musayev F.N., Robinson H., Scarsdale N., et al. Crystal structures of the BlaI repressor from Staphylococcus aureus and its complex with DNA: insights into transcriptional regulation of the bla and mec operons. J. Bacteriol. 187 (2005) 1833-1844
    • (2005) J. Bacteriol. , vol.187 , pp. 1833-1844
    • Safo, M.K.1    Zhao, Q.2    Ko, T.P.3    Musayev, F.N.4    Robinson, H.5    Scarsdale, N.6
  • 57
    • 0036682596 scopus 로고    scopus 로고
    • Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB
    • Selmer M., and Su X.D. Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB. EMBO J. 21 (2002) 4145-4153
    • (2002) EMBO J. , vol.21 , pp. 4145-4153
    • Selmer, M.1    Su, X.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.