메뉴 건너뛰기




Volumn 50, Issue 4, 2003, Pages 1141-1153

ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; ESCHERICHIA COLI PROTEIN; HELIX LOOP HELIX PROTEIN; PROTEIN ACTIVATED RECEPTOR G; UNCLASSIFIED DRUG;

EID: 0344826584     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03750.x     Document Type: Article
Times cited : (76)

References (54)
  • 1
    • 0038501044 scopus 로고    scopus 로고
    • Architecture of the ParF-ParG protein complex involved in procaryotic DNA segregation
    • Barillà, D., and Hayes, F. (2003) Architecture of the ParF-ParG protein complex involved in procaryotic DNA segregation. Mol Microbiol 49: 487-499.
    • (2003) Mol Microbiol , vol.49 , pp. 487-499
    • Barillà, D.1    Hayes, F.2
  • 2
    • 0035956995 scopus 로고    scopus 로고
    • Contributions of distinct quaternary contacts to cooperative operator binding by Mnt repressor
    • Berggrun, A., and Sauer, R.T. (2001) Contributions of distinct quaternary contacts to cooperative operator binding by Mnt repressor. Proc Natl Acad Sci USA 98: 2301-2305.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2301-2305
    • Berggrun, A.1    Sauer, R.T.2
  • 3
    • 0035856287 scopus 로고    scopus 로고
    • The bacterial ParA-ParB partitioning proteins
    • Bignell, C., and Thomas, C.M. (2001) The bacterial ParA-ParB partitioning proteins. J Biotechnol 91: 1-34.
    • (2001) J Biotechnol , vol.91 , pp. 1-34
    • Bignell, C.1    Thomas, C.M.2
  • 4
    • 0033106245 scopus 로고    scopus 로고
    • P1 ParA interacts with the P1 partition complex at parS and an ATP-ADP switch controls ParA activities
    • Bouet, J.Y., and Funnell, B.E. (1999) P1 ParA interacts with the P1 partition complex at parS and an ATP-ADP switch controls ParA activities. EMBO J 18: 1415-1424.
    • (1999) EMBO J , vol.18 , pp. 1415-1424
    • Bouet, J.Y.1    Funnell, B.E.2
  • 5
    • 0025336625 scopus 로고
    • Structure of Arc repressor in solution: Evidence for a family of β-sheet DNA-binding proteins
    • Breg, J.N., van Ophensden, J.H.J., Burgering, M.J.M., Boelens, R., and Kaptein, R. (1990) Structure of Arc repressor in solution: evidence for a family of β-sheet DNA-binding proteins. Nature 346: 586-589.
    • (1990) Nature , vol.346 , pp. 586-589
    • Breg, J.N.1    Van Ophensden, J.H.J.2    Burgering, M.J.M.3    Boelens, R.4    Kaptein, R.5
  • 7
    • 0032697047 scopus 로고    scopus 로고
    • NikR is a ribbon-helix-helix DNA-binding protein
    • Chivers, P.T., and Sauer, R.T. (1999) NikR is a ribbon-helix-helix DNA-binding protein. Protein Sci 8: 2494-2500.
    • (1999) Protein Sci , vol.8 , pp. 2494-2500
    • Chivers, P.T.1    Sauer, R.T.2
  • 8
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 9
    • 12244298896 scopus 로고    scopus 로고
    • F-actin-like filaments formed by plasmid segregation protein ParM
    • van den Ent, F., Moller-Jensen, J., Amos, L.A., Gerdes, K., and Lowe, J. (2002) F-actin-like filaments formed by plasmid segregation protein ParM. EMBO J 21: 6935-6943.
    • (2002) EMBO J , vol.21 , pp. 6935-6943
    • Van Den Ent, F.1    Moller-Jensen, J.2    Amos, L.A.3    Gerdes, K.4    Lowe, J.5
  • 10
    • 0028951040 scopus 로고
    • Comparison of the backbone dynamics of a folded and unfolded SH3 domain existing in equilibrium in aqueous buffer
    • Farrow, N.A., Zhang, O., Forman-Kay, J.D., and Kay, L.E. (1995a) Comparison of the backbone dynamics of a folded and unfolded SH3 domain existing in equilibrium in aqueous buffer. Biochemistry 34: 868-878.
    • (1995) Biochemistry , vol.34 , pp. 868-878
    • Farrow, N.A.1    Zhang, O.2    Forman-Kay, J.D.3    Kay, L.E.4
  • 11
    • 0029367044 scopus 로고
    • Spectral density function mapping using 15N relaxation data exclusively
    • Farrow, N.A., Zhang, O., Szabo, A., Torchia, D.A., and Kay, L.E. (1995b) Spectral density function mapping using 15N relaxation data exclusively. J Biomol NMR 6: 153-162.
    • (1995) J Biomol NMR , vol.6 , pp. 153-162
    • Farrow, N.A.1    Zhang, O.2    Szabo, A.3    Torchia, D.A.4    Kay, L.E.5
  • 12
    • 0037341855 scopus 로고    scopus 로고
    • Productive interaction between the chromosome partitioning proteins, ParA and ParB, is required for the progression of the cell cycle in Caulobacter crescentus
    • Figge, R.M., Easter, J., and Gober, J.W. (2003) Productive interaction between the chromosome partitioning proteins, ParA and ParB, is required for the progression of the cell cycle in Caulobacter crescentus. Mol Microbiol 47: 1225-1237.
    • (2003) Mol Microbiol , vol.47 , pp. 1225-1237
    • Figge, R.M.1    Easter, J.2    Gober, J.W.3
  • 13
    • 0031943805 scopus 로고    scopus 로고
    • A new method to characterize hydrophobic organization of proteins: Application to rational protein engineering of barnase
    • Golovanov, A.P., Efremov, R.G., Jaravine, V.A., Vergoten, G., Kirpichnikov, M.P., and Arseniev, A.S. (1998) A new method to characterize hydrophobic organization of proteins: application to rational protein engineering of barnase. J Biomol Struct Dynam 15: 673-687.
    • (1998) J Biomol Struct Dynam , vol.15 , pp. 673-687
    • Golovanov, A.P.1    Efremov, R.G.2    Jaravine, V.A.3    Vergoten, G.4    Kirpichnikov, M.P.5    Arseniev, A.S.6
  • 14
    • 0035808306 scopus 로고    scopus 로고
    • Structure-activity relationships in flexible protein domains: Regulation of rho GTPases by RhoGDI and D4 GDI
    • Golovanov, A.P., Chuang, T.-H., DerMardirossian, C., Barsukov, I., Hawkins, D., Badii, R., et al. (2001) Structure-activity relationships in flexible protein domains: regulation of rho GTPases by RhoGDI and D4 GDI. J Mol Biol 305: 121-135.
    • (2001) J Mol Biol , vol.305 , pp. 121-135
    • Golovanov, A.P.1    Chuang, T.-H.2    DerMardirossian, C.3    Barsukov, I.4    Hawkins, D.5    Badii, R.6
  • 15
    • 0039985836 scopus 로고    scopus 로고
    • The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator
    • Gomis-Rüth, F.X., Solà, M., Acebo, P., Parraga, A., Guasch, A., Eritja, R., et al. (1998) The structure of plasmid-encoded transcriptional repressor CopG unliganded and bound to its operator. EMBO J 17: 7404-7415.
    • (1998) EMBO J , vol.17 , pp. 7404-7415
    • Gomis-Rüth, F.X.1    Solà, M.2    Acebo, P.3    Parraga, A.4    Guasch, A.5    Eritja, R.6
  • 16
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure
    • Gough, J., Karplus, K., Hughey, R., and Chothia, C. (2001) Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. J Mol Biol 313: 903-919.
    • (2001) J Mol Biol , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 17
    • 0033854632 scopus 로고    scopus 로고
    • The partition system of multidrug resistance plasmid TP228 includes a novel protein that epitomizes an evolutionary distinct subgroup of the ParA superfamily
    • Hayes, F. (2000) The partition system of multidrug resistance plasmid TP228 includes a novel protein that epitomizes an evolutionary distinct subgroup of the ParA superfamily. Mol Microbiol 37: 528-541.
    • (2000) Mol Microbiol , vol.37 , pp. 528-541
    • Hayes, F.1
  • 18
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B.A., and Blevins, R.A. (1994) NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4: 603-614.
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 19
    • 0035980822 scopus 로고    scopus 로고
    • Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120
    • Kaneko, T., Nakamura, Y., Wolk, C.P., Kuritz, T., Sasamoto, S., Watanabe, A., et al. (2001) Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. DNA Res 8: 205-213, 227-253.
    • (2001) DNA Res , vol.8 , pp. 205-213
    • Kaneko, T.1    Nakamura, Y.2    Wolk, C.P.3    Kuritz, T.4    Sasamoto, S.5    Watanabe, A.6
  • 20
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L.E., Keifer, P., and Saarinen, T. (1992a) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114: 10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 22
    • 0033587717 scopus 로고    scopus 로고
    • Gene silencing via protein-mediated subcellular localization of DNA
    • Kim, S.K., and Wang, J.C. (1999) Gene silencing via protein-mediated subcellular localization of DNA. Proc Natl Acad Sci USA 96: 8557-8561.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8557-8561
    • Kim, S.K.1    Wang, J.C.2
  • 23
    • 0024552617 scopus 로고
    • DNA binding specificity of the Arc and Mnt repressors is determined by a short region of N-terminal residues
    • Knight, K.L., and Sauer, R.T. (1989) DNA binding specificity of the Arc and Mnt repressors is determined by a short region of N-terminal residues. Proc Natl Acad Sci USA 86: 797-801.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 797-801
    • Knight, K.L.1    Sauer, R.T.2
  • 24
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • Koonin, E.V. (1993) A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif. J Mol Biol 229: 1165-1174.
    • (1993) J Mol Biol , vol.229 , pp. 1165-1174
    • Koonin, E.V.1
  • 25
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graphics 14: 51-55.
    • (1996) J Mol Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 26
    • 0034997888 scopus 로고    scopus 로고
    • Molecular analysis of the pRA2 partitioning region: ParB autoregulates parAB transcription and forms a nucleoprotein complex with the plasmid partition site, parS
    • Kwong, S.M., Yeo, C.C., and Poh, C.L. (2001) Molecular analysis of the pRA2 partitioning region: ParB autoregulates parAB transcription and forms a nucleoprotein complex with the plasmid partition site, parS. Mol Microbiol 40: 621-633.
    • (2001) Mol Microbiol , vol.40 , pp. 621-633
    • Kwong, S.M.1    Yeo, C.C.2    Poh, C.L.3
  • 27
    • 0036034803 scopus 로고    scopus 로고
    • The P1 plasmid is segregated to daughter cells by a 'capture and ejection' mechanism coordinated with Escherichia coli cell division
    • Li, Y., and Austin, S. (2002) The P1 plasmid is segregated to daughter cells by a 'capture and ejection' mechanism coordinated with Escherichia coli cell division. Mol Microbiol 46: 63-74.
    • (2002) Mol Microbiol , vol.46 , pp. 63-74
    • Li, Y.1    Austin, S.2
  • 28
    • 0037316363 scopus 로고    scopus 로고
    • ARIA: Automated NOE assignment and NMR structure calculation
    • Linge, J.P., Habeck, M., Rieping, W., and Nilges, M. (2003) ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 19: 315-316.
    • (2003) Bioinformatics , vol.19 , pp. 315-316
    • Linge, J.P.1    Habeck, M.2    Rieping, W.3    Nilges, M.4
  • 29
    • 0036965763 scopus 로고    scopus 로고
    • TraY DNA recognition of its two F factor binding sites
    • Lum, P.L., Rodgers, M.E., and Schildbach, J.F. (2002) TraY DNA recognition of its two F factor binding sites. J Mol Biol 321: 563-578.
    • (2002) J Mol Biol , vol.321 , pp. 563-578
    • Lum, P.L.1    Rodgers, M.E.2    Schildbach, J.F.3
  • 30
    • 0033754425 scopus 로고    scopus 로고
    • Complete nucleotide sequence of ubiquitous plasmid pEA29 from Erwinia amylovora strain Ea88: Gene organization and intraspecies variation
    • McGhee, G.C., and Jones, A.L. (2000) Complete nucleotide sequence of ubiquitous plasmid pEA29 from Erwinia amylovora strain Ea88: gene organization and intraspecies variation. Appl Environ Microbiol 66: 4897-4907.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 4897-4907
    • McGhee, G.C.1    Jones, A.L.2
  • 31
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L.J., Bryson, K., and Jones, D.T. (2000) The PSIPRED protein structure prediction server. Bioinformatics 16: 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 32
    • 0034234636 scopus 로고    scopus 로고
    • Plasmid and chromosome segregation in prokaryotes
    • Moller-Jensen, J., Jensen, R.B., and Gerdes, K. (2000) Plasmid and chromosome segregation in prokaryotes. Trends Microbiol 8: 313-320.
    • (2000) Trends Microbiol , vol.8 , pp. 313-320
    • Moller-Jensen, J.1    Jensen, R.B.2    Gerdes, K.3
  • 33
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • Moller-Jensen, J., Jensen, R.B., Lowe, J., and Gerdes, K. (2002) Prokaryotic DNA segregation by an actin-like filament. EMBO J 21: 3119-3127.
    • (2002) EMBO J , vol.21 , pp. 3119-3127
    • Moller-Jensen, J.1    Jensen, R.B.2    Lowe, J.3    Gerdes, K.4
  • 35
    • 0025149275 scopus 로고
    • A family of ATPases involved in active partitioning of diverse bacterial plasmids
    • Motallebi-Veshareh, M., Rouch, D.A., and Thomas, C.M. (1990) A family of ATPases involved in active partitioning of diverse bacterial plasmids. Mol Microbiol 4: 1455-1463.
    • (1990) Mol Microbiol , vol.4 , pp. 1455-1463
    • Motallebi-Veshareh, M.1    Rouch, D.A.2    Thomas, C.M.3
  • 36
    • 0035824885 scopus 로고    scopus 로고
    • Crystal structure of ω transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5 Å resolution
    • Murayama, K., Orth, P., de la Hoz, A.B., Alonso, J.C., and Saenger, W. (2001) Crystal structure of ω transcriptional repressor encoded by Streptococcus pyogenes plasmid pSM19035 at 1.5 Å resolution. J Mol Biol 314: 789-796.
    • (2001) J Mol Biol , vol.314 , pp. 789-796
    • Murayama, K.1    Orth, P.2    De La Hoz, A.B.3    Alonso, J.C.4    Saenger, W.5
  • 37
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from β-spectrin
    • Nilges, M., Macias, M.J., O'Donoghue, S., and Oschkinat, H. (1997) Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from β-spectrin. J Mol Biol 269: 408-422.
    • (1997) J Mol Biol , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    O'Donoghue, S.3    Oschkinat, H.4
  • 38
    • 0036182510 scopus 로고    scopus 로고
    • The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins
    • Oberer, M., Zangger, K., Prytulla, S., and Keller, W. (2002) The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins. Biochem J 361: 41-47.
    • (2002) Biochem J , vol.361 , pp. 41-47
    • Oberer, M.1    Zangger, K.2    Prytulla, S.3    Keller, W.4
  • 39
    • 0036464541 scopus 로고    scopus 로고
    • Identification, cloning and characterization of a new DNA-binding protein from the hyperthermophilic methanogen Methanopyrus kandleri
    • Pavlov, N.A., Cherny, D.I., Nazimov, I.V., Slesarev, A.I., and Subramaniam, V. (2002) Identification, cloning and characterization of a new DNA-binding protein from the hyperthermophilic methanogen Methanopyrus kandleri. Nucleic Acids Res 30: 685-694.
    • (2002) Nucleic Acids Res , vol.30 , pp. 685-694
    • Pavlov, N.A.1    Cherny, D.I.2    Nazimov, I.V.3    Slesarev, A.I.4    Subramaniam, V.5
  • 40
    • 0000660936 scopus 로고
    • Mapping of spectral-density functions using heteronuclear NMR relaxation measurements
    • Peng, J.W., and Wagner, G. (1992) Mapping of spectral-density functions using heteronuclear NMR relaxation measurements. J Magn Reson 98: 308-332.
    • (1992) J Magn Reson , vol.98 , pp. 308-332
    • Peng, J.W.1    Wagner, G.2
  • 41
    • 0024462909 scopus 로고
    • Three-dimensional crystal structures of Escherichia coli Met repressor with and without corepressor
    • Rafferty, J.B., Somers, W.S., Saint-Girons, I., and Phillips, S.E.V. (1989) Three-dimensional crystal structures of Escherichia coli Met repressor with and without corepressor. Nature 341: 705-710.
    • (1989) Nature , vol.341 , pp. 705-710
    • Rafferty, J.B.1    Somers, W.S.2    Saint-Girons, I.3    Phillips, S.E.V.4
  • 42
    • 0028177303 scopus 로고
    • DNA recognition by β-sheets in the Arc repressor-operator crystal structure
    • Raumann, B.E., Rould, M.A., Pabo, C.O., and Sauer, R.T. (1994) DNA recognition by β-sheets in the Arc repressor-operator crystal structure. Nature 367: 754-757.
    • (1994) Nature , vol.367 , pp. 754-757
    • Raumann, B.E.1    Rould, M.A.2    Pabo, C.O.3    Sauer, R.T.4
  • 43
    • 0028843773 scopus 로고
    • Dramatic changes in DNA-binding specificity caused by single residue substitution in an Arc/Mnt hybrid repressor
    • Raumann, B.E., Knight, K.L., and Sauer, R.T. (1995) Dramatic changes in DNA-binding specificity caused by single residue substitution in an Arc/Mnt hybrid repressor. Nature Struct Biol 2: 1115-1122.
    • (1995) Nature Struct Biol , vol.2 , pp. 1115-1122
    • Raumann, B.E.1    Knight, K.L.2    Sauer, R.T.3
  • 44
    • 0027732050 scopus 로고
    • Characteristics and significance of DNA binding activity of plasmid stabilization protein ParD from the broad host-range plasmid RK2
    • Roberts, R.C., Spangler, C., and Helinski, D.R. (1993) Characteristics and significance of DNA binding activity of plasmid stabilization protein ParD from the broad host-range plasmid RK2. J Biol Chem 268: 27109-27117.
    • (1993) J Biol Chem , vol.268 , pp. 27109-27117
    • Roberts, R.C.1    Spangler, C.2    Helinski, D.R.3
  • 45
    • 0033593587 scopus 로고    scopus 로고
    • Silencing of genes flanking the P1 plasmid centromere
    • Rodionov, O., Lobocka, M., and Yarmolinsky, M. (1999) Silencing of genes flanking the P1 plasmid centromere. Science 283: 546-549.
    • (1999) Science , vol.283 , pp. 546-549
    • Rodionov, O.1    Lobocka, M.2    Yarmolinsky, M.3
  • 46
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and Blundell, T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 47
    • 0028952291 scopus 로고
    • Crystal structure, folding and operator binding of the hyperstable Arc repressor mutant PL8
    • Schildbach, J.F., Milla, M.E., Jefferey, P.D., Raumann, B.E., and Sauer, R.T. (1995) Crystal structure, folding and operator binding of the hyperstable Arc repressor mutant PL8. Biochemistry 34: 1405-1412.
    • (1995) Biochemistry , vol.34 , pp. 1405-1412
    • Schildbach, J.F.1    Milla, M.E.2    Jefferey, P.D.3    Raumann, B.E.4    Sauer, R.T.5
  • 48
    • 0033514299 scopus 로고    scopus 로고
    • Origins of DNA-binding specificity: Role of protein contacts with the DNA backbone
    • Schildbach, J.F., Karzai, A.W., Raumann, B.E., and Sauer, R.T. (1999) Origins of DNA-binding specificity: role of protein contacts with the DNA backbone. Proc Natl Acad Sci USA 96: 811-817.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 811-817
    • Schildbach, J.F.1    Karzai, A.W.2    Raumann, B.E.3    Sauer, R.T.4
  • 49
    • 0037115830 scopus 로고    scopus 로고
    • Specificity of Mnt 'master residue' obtained from in vivo and in vitro selections
    • Silbaq, F.S., Ruttenberg, S.E., and Stormo, G.D. (2002) Specificity of Mnt 'master residue' obtained from in vivo and in vitro selections. Nucleic Acids Res 30: 5539-5548.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5539-5548
    • Silbaq, F.S.1    Ruttenberg, S.E.2    Stormo, G.D.3
  • 50
    • 0036723823 scopus 로고    scopus 로고
    • A genetically economical family of plasmid-encoded transcriptional repressors involved in control of plasmid copy number
    • del Solar, G., Hernández-Arriaga, A.M., Gomis-Rüth, F.X., Coll, M., and Espinosa, M. (2002) A genetically economical family of plasmid-encoded transcriptional repressors involved in control of plasmid copy number. J Bacteriol 184: 4943-4951.
    • (2002) J Bacteriol , vol.184 , pp. 4943-4951
    • Del Solar, G.1    Hernández-Arriaga, A.M.2    Gomis-Rüth, F.X.3    Coll, M.4    Espinosa, M.5
  • 51
    • 0026641755 scopus 로고
    • Crystal structure of the Met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by β-strands
    • Somers, W.S., and Phillips, S.E.V. (1992) Crystal structure of the Met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by β-strands. Nature 359: 387-393.
    • (1992) Nature , vol.359 , pp. 387-393
    • Somers, W.S.1    Phillips, S.E.V.2
  • 52
    • 0029564595 scopus 로고
    • Are buried salt-bridges important for protein stability and conformational specificity?
    • Waldburger, C.D., Schildbach, J.F., and Sauer, R.T. (1995) Are buried salt-bridges important for protein stability and conformational specificity? Nature Struct Biol 2: 122-128.
    • (1995) Nature Struct Biol , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.