메뉴 건너뛰기




Volumn 7, Issue 9, 1998, Pages 1875-1883

Conversion of a β-strand to an α-helix induced by a single-site mutation observed in the crystal structure of Fis mutant Pro26 Ala

Author keywords

Conformational change; Hinge proline; Secondary structural change; X ray diffraction

Indexed keywords

ALANINE; AMINO ACID; BACTERIAL PROTEIN; CYSTEINE; GLUTAMIC ACID; LYSINE; MUTANT PROTEIN; PROLINE; SERINE;

EID: 0031713107     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070904     Document Type: Article
Times cited : (36)

References (39)
  • 2
    • 0023818750 scopus 로고
    • Replacement of Pro-86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability
    • Alber T, Bell JA, Sun D-P, Nicholson H, Wozniak JA, Cook S, Matthews BW. 1988. Replacement of Pro-86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability. Science 239:631-635.
    • (1988) Science , vol.239 , pp. 631-635
    • Alber, T.1    Bell, J.A.2    Sun, D.-P.3    Nicholson, H.4    Wozniak, J.A.5    Cook, S.6    Matthews, B.W.7
  • 3
    • 0025766646 scopus 로고
    • Efficient excision of phage lambda from the Escherichia coli chromosome requires the Fis protein
    • Ball BA, Johnson RC. 1991. Efficient excision of phage lambda from the Escherichia coli chromosome requires the Fis protein. J Bacteriol 173:4027-4031.
    • (1991) J Bacteriol , vol.173 , pp. 4027-4031
    • Ball, B.A.1    Johnson, R.C.2
  • 5
    • 0027236794 scopus 로고
    • Structural basis of amino acid α helix propensity
    • Blaber M, Zhang X-J, Matthews BW. 1993. Structural basis of amino acid α helix propensity. Science 260:1637-1640.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.-J.2    Matthews, B.W.3
  • 6
    • 0029020484 scopus 로고
    • N- and C-capping preferences for all 20 amino acids in α-helical peptide
    • Doig AJ, Baldwin RL. 1995. N-and C-capping preferences for all 20 amino acids in α-helical peptide. Protein Sci 4:1325-1336.
    • (1995) Protein Sci , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 8
    • 0026470852 scopus 로고
    • The Fis protein: It's not just for DNA inversion anymore
    • Finkel SE, Johnson RC. 1992. The Fis protein: It's not just for DNA inversion anymore. Mol Microbiol 6:3257-3265.
    • (1992) Mol Microbiol , vol.6 , pp. 3257-3265
    • Finkel, S.E.1    Johnson, R.C.2
  • 10
    • 0025040403 scopus 로고
    • The Hin invertasome: Protein-mediated joining of distant recombination sites at the enhancer
    • Heichman KA, Johnson RC. 1990. The Hin invertasome: Protein-mediated joining of distant recombination sites at the enhancer. Science 249:511-517.
    • (1990) Science , vol.249 , pp. 511-517
    • Heichman, K.A.1    Johnson, R.C.2
  • 11
    • 0028174643 scopus 로고
    • Quantitative determination of helical propensities from trifluoroethanol titration curves
    • Jasanoff A, Fersht AR. 1994. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry 33:2129-2135.
    • (1994) Biochemistry , vol.33 , pp. 2129-2135
    • Jasanoff, A.1    Fersht, A.R.2
  • 12
    • 0026235924 scopus 로고
    • Mechanism of site-specific DNA inversion in bacteria
    • Johnson R. 1991. Mechanism of site-specific DNA inversion in bacteria. Curr Opin Gen Devel 1:404-411.
    • (1991) Curr Opin Gen Devel , vol.1 , pp. 404-411
    • Johnson, R.1
  • 13
    • 0022545522 scopus 로고
    • Host protein requirements for in vitro site-specific DNA inversion
    • Johnson RC, Bruist MF, Simon MI. 1986. Host protein requirements for in vitro site-specific DNA inversion. Cell 46:531-539.
    • (1986) Cell , vol.46 , pp. 531-539
    • Johnson, R.C.1    Bruist, M.F.2    Simon, M.I.3
  • 14
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • Kelly JW. 1996. Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 6:11-17.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 15
    • 0023009072 scopus 로고
    • Purification and properties of the Escherichia coli host factor required for inversion of the G segment in bacteriophage Mu
    • Koch C, Kahmann R. 1986. Purification and properties of the Escherichia coli host factor required for inversion of the G segment in bacteriophage Mu. J Biol Chem 261:15673-15678.
    • (1986) J Biol Chem , vol.261 , pp. 15673-15678
    • Koch, C.1    Kahmann, R.2
  • 16
    • 0025950160 scopus 로고
    • The N-terminal part of the E. coli. DNA binding protein Fis is essential for stimulating site-specific DNA inversion but is not required for specific DNA binding
    • Koch C, Ninnemann O, Fuss H, Kahmann R. 1991. The N-terminal part of the E. coli. DNA binding protein Fis is essential for stimulating site-specific DNA inversion but is not required for specific DNA binding. Nucleic Acids Res 19:5915-5922.
    • (1991) Nucleic Acids Res , vol.19 , pp. 5915-5922
    • Koch, C.1    Ninnemann, O.2    Fuss, H.3    Kahmann, R.4
  • 18
    • 0026749182 scopus 로고
    • Crystal structure of the Factor for Inversion Stimulation FIS at 2.0 Å resolution
    • Kostrewa D, Granzin J, Stock D, Choe H-C, Labahn J, Saenger W. 1992. Crystal structure of the Factor for Inversion Stimulation FIS at 2.0 Å resolution. J Mol Biol 226:209-226.
    • (1992) J Mol Biol , vol.226 , pp. 209-226
    • Kostrewa, D.1    Granzin, J.2    Stock, D.3    Choe, H.-C.4    Labahn, J.5    Saenger, W.6
  • 19
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24:946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 20
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt O, Grunert H, Hahn U. 1990. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene 96:125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.2    Hahn, U.3
  • 21
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 22
    • 0030816685 scopus 로고    scopus 로고
    • Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water
    • Luo P, Baldwin RL. 1997. Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 38:8413-8421.
    • (1997) Biochemistry , vol.38 , pp. 8413-8421
    • Luo, P.1    Baldwin, R.L.2
  • 23
    • 0027998757 scopus 로고
    • Context is a major determinant of β-sheet propensity
    • Minor DL, Kim PS. 1994. Context is a major determinant of β-sheet propensity. Nature 371:264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor, D.L.1    Kim, P.S.2
  • 24
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor DL, Kim PS. 1996. Context-dependent secondary structure formation of a designed protein sequence. Nature 380:730-734.
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor, D.L.1    Kim, P.S.2
  • 25
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Nell KT, DeGrado WF. 1990. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250:646-651.
    • (1990) Science , vol.250 , pp. 646-651
    • O'Nell, K.T.1    Degrado, W.F.2
  • 26
    • 0025905172 scopus 로고
    • Identification of two functional regions in Fis: The N-terminus is required to promote Hin-mediated DNA inversion but not lambda excision
    • Osuna R, Finkel SE, Johnson RC. 1991. Identification of two functional regions in Fis: The N-terminus is required to promote Hin-mediated DNA inversion but not lambda excision. EMBO J 10:1593-1603.
    • (1991) EMBO J , vol.10 , pp. 1593-1603
    • Osuna, R.1    Finkel, S.E.2    Johnson, R.C.3
  • 27
    • 19244372639 scopus 로고    scopus 로고
    • Variable structures of Fis-DNA complexes determined by flanking DNA contacts
    • Pan, CQ, Finkel SE, Cramton SE, Sigman DS, Johnson RC. 1996. Variable structures of Fis-DNA complexes determined by flanking DNA contacts. J Mol Biol 264:675-695.
    • (1996) J Mol Biol , vol.264 , pp. 675-695
    • Pan, C.Q.1    Finkel, S.E.2    Cramton, S.E.3    Sigman, D.S.4    Johnson, R.C.5
  • 28
    • 0028782016 scopus 로고
    • Molecular biology and genetics of prion disease
    • Prusiner SB. 1994. Molecular biology and genetics of prion disease. Phil Trans R Soc Lond B 343:447-463.
    • (1994) Phil Trans R Soc Lond B , vol.343 , pp. 447-463
    • Prusiner, S.B.1
  • 29
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α helix
    • Richardson JS, Richardson DC. 1988. Amino acid preferences for specific locations at the ends of α helix. Science 240:1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 31
    • 0030842186 scopus 로고    scopus 로고
    • The transactivation region of the Fis protein that controls site-specific DNA inversion contains extended mobile β-hairpin arms
    • Safo MK, Yang WZ, Corselli L, Cramton SE, Yuan HS, Johnson RC. 1997. The transactivation region of the Fis protein that controls site-specific DNA inversion contains extended mobile β-hairpin arms. EMBO J 16:6860-6873.
    • (1997) EMBO J , vol.16 , pp. 6860-6873
    • Safo, M.K.1    Yang, W.Z.2    Corselli, L.3    Cramton, S.E.4    Yuan, H.S.5    Johnson, R.C.6
  • 32
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama N, Woody RW. 1993. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal Biochem 209:32.
    • (1993) Anal Biochem , vol.209 , pp. 32
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 0032509980 scopus 로고    scopus 로고
    • Crystal structure of the yeast MATα2/MCM1/DNA ternary complex
    • Tan S, Richmond TJ. 1998. Crystal structure of the yeast MATα2/MCM1/DNA ternary complex. Nature 391:660-666.
    • (1998) Nature , vol.391 , pp. 660-666
    • Tan, S.1    Richmond, T.J.2
  • 34
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure in proteins
    • Waterhous VD, Johnson CW. 1994. Importance of environment in determining secondary structure in proteins. Biochemistry 33:2121-2128.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, V.D.1    Johnson, C.W.2
  • 35
    • 0021268779 scopus 로고
    • The locus of sequence-directed and protein-induced DNA bending
    • Wu HM, Crothers DM. 1984. The locus of sequence-directed and protein-induced DNA bending. Nature 308:509-513.
    • (1984) Nature , vol.308 , pp. 509-513
    • Wu, H.M.1    Crothers, D.M.2
  • 36
    • 0029064713 scopus 로고
    • Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
    • Xiong H, Buckwalter BL, Shieh H-M, Kecht MH. 1995. Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proc Natl Acad Sci USA 92:6349-6353.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6349-6353
    • Xiong, H.1    Buckwalter, B.L.2    Shieh, H.-M.3    Kecht, M.H.4
  • 37
    • 0029010741 scopus 로고
    • aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp
    • Xu J, Johnson RC. 1995. aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp. J Bacteriol 177:3166-3175.
    • (1995) J Bacteriol , vol.177 , pp. 3166-3175
    • Xu, J.1    Johnson, R.C.2
  • 38
    • 0027986785 scopus 로고
    • The structure of Fis mutant Pro61-Ala illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue
    • Yuan HS, Wang SS, Yang W-Z, Finkel SE, Johnson, RC. 1994. The structure of Fis mutant Pro61-Ala illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue. J Biol Chem 269:28947-28954.
    • (1994) J Biol Chem , vol.269 , pp. 28947-28954
    • Yuan, H.S.1    Wang, S.S.2    Yang, W.-Z.3    Finkel, S.E.4    Johnson, R.C.5
  • 39
    • 0025939520 scopus 로고
    • The molecular structure of wild-type and a mutant Fis: Relationship between mutational changes and recombinational enhancer function or DNA bending
    • Yuan SH, Finkel SE, Feng JA, Kaczor-Grezskowiak M, Johnson RC, Dickerson RE. 1991. The molecular structure of wild-type and a mutant Fis: Relationship between mutational changes and recombinational enhancer function or DNA bending. Proc Natl Acad Sci USA 88:9558-9562.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9558-9562
    • Yuan, S.H.1    Finkel, S.E.2    Feng, J.A.3    Kaczor-Grezskowiak, M.4    Johnson, R.C.5    Dickerson, R.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.