메뉴 건너뛰기




Volumn 6, Issue 6, 1997, Pages 1237-1247

Secondary and tertiary structural changes in γδ resolvase: Comparison of the wild-type enzyme, the I110R mutant, and the C-terminal DNA binding domain in solution

Author keywords

DNA; Folding; Interaction; NMR; Protein; Recombination; Resolvase; Structure

Indexed keywords

BETA FRUCTOFURANOSIDASE; MUTANT PROTEIN; PROTEIN SUBUNIT; RESOLVASE;

EID: 0030979781     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060612     Document Type: Article
Times cited : (15)

References (25)
  • 1
    • 0021362101 scopus 로고
    • Cleavage of the site-specific recombination protein, γδ resolvase: The smaller of the two fragments binds DNA specifically
    • Abdel-Meguid SS, Grindley NDF, Templeton NS, Steitz TA. 1984. Cleavage of the site-specific recombination protein, γδ resolvase: The smaller of the two fragments binds DNA specifically. Proc Natl Acad Sci USA 81:2001-2005.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 2001-2005
    • Abdel-Meguid, S.S.1    Grindley, N.D.F.2    Templeton, N.S.3    Steitz, T.A.4
  • 2
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C, Xia T, Billeter M, Güntert P, Wüthrich K. 1995. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomol NMR 6:1-10.
    • (1995) J Biomol NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 3
    • 0029360491 scopus 로고
    • Cooperative binding of Tn3 resolvase monomers to a functionally asymmetric binding site
    • Blake DG, Boocock MR, Sherratt DJ, Stark WM. 1995. Cooperative binding of Tn3 resolvase monomers to a functionally asymmetric binding site. Curr Biol 5:1036-1046.
    • (1995) Curr Biol , vol.5 , pp. 1036-1046
    • Blake, D.G.1    Boocock, M.R.2    Sherratt, D.J.3    Stark, W.M.4
  • 4
    • 0028826454 scopus 로고
    • Catalytic residues of γδ resolvase act in cis
    • Boocock MR, Xuewei Z, Grindley NDF. 1995. Catalytic residues of γδ resolvase act in cis. EMBO J 14:5129-5140.
    • (1995) EMBO J , vol.14 , pp. 5129-5140
    • Boocock, M.R.1    Xuewei, Z.2    Grindley, N.D.F.3
  • 5
    • 0025757134 scopus 로고
    • Two-, three-, and four-dimensional NMR methods for obtaining larger and more precise three-dimensional structures of proteins in solution
    • Clore GM, Gronenborn AM. 1991. Two-, three-, and four-dimensional NMR methods for obtaining larger and more precise three-dimensional structures of proteins in solution. Annu Rev Biophys Chem 20:29-63.
    • (1991) Annu Rev Biophys Chem , vol.20 , pp. 29-63
    • Clore, G.M.1    Gronenborn, A.M.2
  • 6
    • 0021781318 scopus 로고
    • Transpositional recombination in prokaryotes
    • Grindley NDF, Reed RR. 1985. Transpositional recombination in prokaryotes. Annu Rev Biochem 54:863-896.
    • (1985) Annu Rev Biochem , vol.54 , pp. 863-896
    • Grindley, N.D.F.1    Reed, R.R.2
  • 7
    • 0029945313 scopus 로고    scopus 로고
    • Flexibility of DNA binding domain of trp repressor required for recognition of different operator sequences
    • Gryk MR, Jardetzky O, Klig LS, Yanofsky C. 1996. Flexibility of DNA binding domain of trp repressor required for recognition of different operator sequences. Protein Sci 5:1195-1197.
    • (1996) Protein Sci , vol.5 , pp. 1195-1197
    • Gryk, M.R.1    Jardetzky, O.2    Klig, L.S.3    Yanofsky, C.4
  • 8
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • Grzesiek S, Bax A. 1992. Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein. J Mag Res 96:432-440.
    • (1992) J Mag Res , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 10
    • 0027470186 scopus 로고
    • Protein-protein interactions directing resolvase site-specific recombination: A structure function analysis
    • Hughes RE, Rice PA, Steitz TA, Grindley NDF. 1993. Protein-protein interactions directing resolvase site-specific recombination: A structure function analysis. EMBO J 12:1447-1458.
    • (1993) EMBO J , vol.12 , pp. 1447-1458
    • Hughes, R.E.1    Rice, P.A.2    Steitz, T.A.3    Grindley, N.D.F.4
  • 11
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T. 1992. 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
  • 12
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A, Ernst RR, Wüthrich K. 1980. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem Biophys Res Commun 95:1-6.
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 13
    • 0028023897 scopus 로고
    • Determination of the structure of the DNA binding domain of γδ resolvase in solution
    • Liu T, DeRose EF, Mullen GP. 1994. Determination of the structure of the DNA binding domain of γδ resolvase in solution. Protein Sci 3:1286-1295.
    • (1994) Protein Sci , vol.3 , pp. 1286-1295
    • Liu, T.1    DeRose, E.F.2    Mullen, G.P.3
  • 14
    • 0342457390 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling: Application to the study of hydrogen exchange in proteins
    • Marion D, Ikura M, Tschudin R, Bax A. 1989. Rapid recording of 2D NMR spectra without phase cycling: Application to the study of hydrogen exchange in proteins. J Magn Reson 48:286-292.
    • (1989) J Magn Reson , vol.48 , pp. 286-292
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 15
    • 0030593482 scopus 로고    scopus 로고
    • Site-specific recombination by Tn3 resolvase, photocrosslinked to its supercoiled DNA substrate
    • Mcllwraith MJ, Boocock MR, Stark WM. 1996. Site-specific recombination by Tn3 resolvase, photocrosslinked to its supercoiled DNA substrate. J Mol Biol 260:299-303.
    • (1996) J Mol Biol , vol.260 , pp. 299-303
    • Mcllwraith, M.J.1    Boocock, M.R.2    Stark, W.M.3
  • 16
    • 0028209323 scopus 로고
    • Model for a DNA-mediated synaptic complex suggested by crystal packing of γδ resolvase subunits
    • Rice PA, Steitz TA. 1994. Model for a DNA-mediated synaptic complex suggested by crystal packing of γδ resolvase subunits. EMBO J 13:1514-1524.
    • (1994) EMBO J , vol.13 , pp. 1514-1524
    • Rice, P.A.1    Steitz, T.A.2
  • 17
    • 0025678617 scopus 로고
    • The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution
    • Sanderson MR, Freemont PS, Rice PA, Goldman A, Hatfull GF, Grindley NDF, Steitz TA. 1990. The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution. Cell 63:1323-1329.
    • (1990) Cell , vol.63 , pp. 1323-1329
    • Sanderson, M.R.1    Freemont, P.S.2    Rice, P.A.3    Goldman, A.4    Hatfull, G.F.5    Grindley, N.D.F.6    Steitz, T.A.7
  • 18
    • 0025946533 scopus 로고
    • Resolvase-catalysed reactions between res sites differing in the central dinucleotide of subsite I
    • Stark WM, Grindley NDF, Hatfull GF, Boocock MR. 1991. Resolvase-catalysed reactions between res sites differing in the central dinucleotide of subsite I. EMBO J 10:3541-3548.
    • (1991) EMBO J , vol.10 , pp. 3541-3548
    • Stark, W.M.1    Grindley, N.D.F.2    Hatfull, G.F.3    Boocock, M.R.4
  • 19
    • 0024364817 scopus 로고
    • Site-specific recombination by Tn3 resolvase: Topological changes in the forward and reverse reactions
    • Stark WM, Sherratt DJ, Boocock MR. 1989. Site-specific recombination by Tn3 resolvase: Topological changes in the forward and reverse reactions. Cell 58:779-790.
    • (1989) Cell , vol.58 , pp. 779-790
    • Stark, W.M.1    Sherratt, D.J.2    Boocock, M.R.3
  • 20
    • 0029664417 scopus 로고    scopus 로고
    • Rate and selectivity of synapsis of res recombination sites by Tn3 resolvase
    • Watson MA, Boocock MR, Stark WM. 1996. Rate and selectivity of synapsis of res recombination sites by Tn3 resolvase. J Mol Biol 257:317-329.
    • (1996) J Mol Biol , vol.257 , pp. 317-329
    • Watson, M.A.1    Boocock, M.R.2    Stark, W.M.3
  • 24
    • 0029127032 scopus 로고
    • Crystal structure of the site-specific recombinase γδ resolvase complexed with a 34 bp cleavage site
    • Yang W, Steitz TA. 1995. Crystal structure of the site-specific recombinase γδ resolvase complexed with a 34 bp cleavage site. Cell 82:193-207.
    • (1995) Cell , vol.82 , pp. 193-207
    • Yang, W.1    Steitz, T.A.2
  • 25
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4:845-858.
    • (1994) J Biomol NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Oliver, J.P.3    Forman-Kay, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.