메뉴 건너뛰기




Volumn 12, Issue 1, 2004, Pages 157-168

Origins of Protein Stability Revealed by Comparing Crystal Structures of TATA Binding Proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; TATA BINDING PROTEIN;

EID: 1642436654     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.12.003     Document Type: Article
Times cited : (14)

References (47)
  • 2
    • 1642480431 scopus 로고
    • On the interpretation of X-ray, single crystal, rotation photographs
    • Bernal J.D. On the interpretation of X-ray, single crystal, rotation photographs. Proc. Royal Soc. (London) A. 113:1926;117-160.
    • (1926) Proc. Royal Soc. (London) a , vol.113 , pp. 117-160
    • Bernal, J.D.1
  • 3
    • 0001644632 scopus 로고
    • Between objectivity and subjectivity
    • Brändén C.-I., Jones T.A. Between objectivity and subjectivity. Nature. 343:1990;687-689.
    • (1990) Nature , vol.343 , pp. 687-689
    • Brändén, C.-I.1    Jones, T.A.2
  • 4
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A.T. Free R value. a novel statistical quantity for assessing the accuracy of crystal structures Nature. 355:1992;472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 5
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger A.T., Kuriyan J., Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 235:1987;458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 8
    • 0027250617 scopus 로고
    • Crystal structure of yeast TATA-binding protein and model for interaction with DNA
    • Chasman D.I., Flaherty K.M., Sharp P.A., Kornberg R.D. Crystal structure of yeast TATA-binding protein and model for interaction with DNA. Proc. Natl. Acad. Sci. USA. 90:1993;8174-8178.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8174-8178
    • Chasman, D.I.1    Flaherty, K.M.2    Sharp, P.A.3    Kornberg, R.D.4
  • 9
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4) the CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project Number 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 10
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly M.L. The molecular surface package. J. Mol. Graph. 11:1993;139-141.
    • (1993) J. Mol. Graph. , vol.11 , pp. 139-141
    • Connolly, M.L.1
  • 13
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A. 47:1991;392-400.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 15
    • 0001912876 scopus 로고
    • Thermoadaptation of methanogenic bacteria by intracellular ion concentration
    • Hensel R., König H. Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 49:1988;75-79.
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 75-79
    • Hensel, R.1    König, H.2
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zhou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: A 'traffic rule' for hot roads
    • Karshikoff A., Ladenstein R. Ion pairs and the thermotolerance of proteins from hyperthermophiles. a 'traffic rule' for hot roads Trends Biochem. Sci. 26:2001;550-556.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 20
    • 0027504913 scopus 로고
    • Crystal structure of a yeast TBP/TATA-box complex
    • Kim Y., Geigler J.H., Hahn S., Sigler P.B. Crystal structure of a yeast TBP/TATA-box complex. Nature. 365:1993;512-520.
    • (1993) Nature , vol.365 , pp. 512-520
    • Kim, Y.1    Geigler, J.H.2    Hahn, S.3    Sigler, P.B.4
  • 21
    • 0031562901 scopus 로고    scopus 로고
    • The 2.1-Å crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box
    • Kosa P.F., Ghosh G., DeDecker B.S., Sigler P.B. The 2.1-Å crystal structure of an archaeal preinitiation complex. TATA-box-binding protein/transcription factor (II)B core/TATA-box Proc. Natl. Acad. Sci. USA. 94:1997;6042-6047.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6042-6047
    • Kosa, P.F.1    Ghosh, G.2    Dedecker, B.S.3    Sigler, P.B.4
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • Lamzin V.S., Wilson K.S. Automated refinement for protein crystallography. Methods Enzymol. 277:1997;269-305.
    • (1997) Methods Enzymol. , vol.277 , pp. 269-305
    • Lamzin, V.S.1    Wilson, K.S.2
  • 24
  • 25
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., Richards F.M. The interpretation of protein structures. estimation of static accessibility J. Mol. Biol. 55:1971;379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 26
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: Structural basis for thermostability
    • Lim J.-H., Yu Y.G., Han Y.S., Cho S., Ahn B.-Y., Kim S.-H., Cho Y. The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution. structural basis for thermostability J. Mol. Biol. 270:1997;259-274.
    • (1997) J. Mol. Biol. , vol.270 , pp. 259-274
    • Lim, J.-H.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.4    Ahn, B.-Y.5    Kim, S.-H.6    Cho, Y.7
  • 27
    • 0033598826 scopus 로고    scopus 로고
    • The structural basis for the oriented assembly of a TBP/TFB/promoter complex
    • Littlefield O., Korkhin Y., Sigler P.B. The structural basis for the oriented assembly of a TBP/TFB/promoter complex. Proc. Natl. Acad. Sci. USA. 96:1999;13668-13673.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13668-13673
    • Littlefield, O.1    Korkhin, Y.2    Sigler, P.B.3
  • 28
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I.K., Thornton J.M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:1994;777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 32
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-liklihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-liklihood method. Acta Crystallogr. D. 53:1997;240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 0015520434 scopus 로고
    • The effects of salts on the free energies of nonpolar groups in model peptides
    • Nandi P.K., Robinson D.R. The effects of salts on the free energies of nonpolar groups in model peptides. J. Am. Chem. Soc. 94:1972;1308-1315.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 1308-1315
    • Nandi, P.K.1    Robinson, D.R.2
  • 34
    • 84920325457 scopus 로고
    • AMore: An automated package for molecular replacement
    • Navaza J. AMore. an automated package for molecular replacement Acta Crystallogr. A. 50:1994;157-163.
    • (1994) Acta Crystallogr. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 35
    • 0028056035 scopus 로고
    • 2.1 Å resolution refined structure of a TATA box-binding protein(TBP)
    • Nikolov D.B., Burley S.K. 2.1 Å resolution refined structure of a TATA box-binding protein(TBP). Nat. Struct. Biol. 1:1994;621-637.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 621-637
    • Nikolov, D.B.1    Burley, S.K.2
  • 37
    • 0033573008 scopus 로고    scopus 로고
    • TATA element recognition by the TATA box-binding protein has been conserved throughout evolution
    • Patikoglou G.A., Kim J.L., Sun L., Yang S.-H., Kodadek T., Burley S.K. TATA element recognition by the TATA box-binding protein has been conserved throughout evolution. Genes Dev. 13:1999;3217-3230.
    • (1999) Genes Dev. , vol.13 , pp. 3217-3230
    • Patikoglou, G.A.1    Kim, J.L.2    Sun, L.3    Yang, S.-H.4    Kodadek, T.5    Burley, S.K.6
  • 40
    • 84944817135 scopus 로고
    • The molecular replacement method
    • Rossmann M.G. The molecular replacement method. Acta Crystallogr. A. 46:1990;73-82.
    • (1990) Acta Crystallogr. a , vol.46 , pp. 73-82
    • Rossmann, M.G.1
  • 41
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetryc unit
    • Rossmann M.G., Blow D.M. The detection of sub-units within the crystallographic asymmetryc unit. Acta Crystallogr. 15:1962;24-31.
    • (1962) Acta Crystallogr. , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 45
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanims for thermostability
    • Vieille C., Zeikus G.J. Hyperthermophilic enzymes. sources, uses, and molecular mechanims for thermostability Microbiol. Mol. Biol. Rev. 65:2001;1-43.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 47
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm B.H., Bragg J.K. Theory of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31:1959;526-535.
    • (1959) J. Chem. Phys. , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.