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Volumn 7, Issue 9, 1998, Pages 1939-1946

The de novo design of a rubredoxin-like Fe site

Author keywords

De novo design; Metalloprotein; Protein engineering; Rubredoxin

Indexed keywords

CADMIUM; COBALT; CYSTEINE; FERRIC ION; METAL; MUTANT PROTEIN; PROTEIN G; RUBREDOXIN;

EID: 0031694147     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070909     Document Type: Article
Times cited : (57)

References (65)
  • 1
    • 2742516196 scopus 로고
    • Novel iron-sulfur centers in metalloenzymes and redox proteins from extreme thermophilic bacteria
    • Adams M. 1992. Novel iron-sulfur centers in metalloenzymes and redox proteins from extreme thermophilic bacteria. Adv Inorg Chem 38:341-396.
    • (1992) Adv Inorg Chem , vol.38 , pp. 341-396
    • Adams, M.1
  • 2
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • Baldwin EP, Hajiseyedjavadi O, Basse WA, Matthews BW. 1993. The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science 262:1715-1718.
    • (1993) Science , vol.262 , pp. 1715-1718
    • Baldwin, E.P.1    Hajiseyedjavadi, O.2    Basse, W.A.3    Matthews, B.W.4
  • 3
    • 0002746714 scopus 로고    scopus 로고
    • Polypeptides with supersecondary structures as templates in rational catalyst design. Catalysis of self functionalization by designed helix-loop-helix motifs
    • Baltzer L, Lundh A-C, Broo K, Olofsson S, Ahlberg P. 1996. Polypeptides with supersecondary structures as templates in rational catalyst design. Catalysis of self functionalization by designed helix-loop-helix motifs. J Chem Soc Perkin Trans 2:1671-1676.
    • (1996) J Chem Soc Perkin Trans , vol.2 , pp. 1671-1676
    • Baltzer, L.1    Lundh, A.-C.2    Broo, K.3    Olofsson, S.4    Ahlberg, P.5
  • 5
    • 0023644319 scopus 로고
    • The electronic and magnetic properties of rubredoxin: A low-temperature magnetic circular dichroism study
    • Bennett DE, Johnson MK. 1987. The electronic and magnetic properties of rubredoxin: A low-temperature magnetic circular dichroism study. Biochim Biophys Acta 911:71-90.
    • (1987) Biochim Biophys Acta , vol.911 , pp. 71-90
    • Bennett, D.E.1    Johnson, M.K.2
  • 6
    • 0032546610 scopus 로고    scopus 로고
    • Benson et al. 1998. Biochemistry 37:7070-7076.
    • (1998) Biochemistry , vol.37 , pp. 7070-7076
    • Benson1
  • 7
    • 0026347331 scopus 로고
    • Determinants of protein hyperthermostability: Purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR
    • Blake PR, Park J, Bryant FO, Aono S, Magnuson JK, Eccleston E, Howard JB, Summers MF, Adams MWW. 1991. Determinants of protein hyperthermostability: Purification and amino acid sequence of rubredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus and secondary structure of the zinc adduct by NMR. Biochemistry 30:10885-10895.
    • (1991) Biochemistry , vol.30 , pp. 10885-10895
    • Blake, P.R.1    Park, J.2    Bryant, F.O.3    Aono, S.4    Magnuson, J.K.5    Eccleston, E.6    Howard, J.B.7    Summers, M.F.8    Adams, M.W.W.9
  • 10
    • 84943509794 scopus 로고
    • Direct formation of peptide analogues of rubredoxin and four-iron ferredoxins from their components
    • Christou G, Ridge B, Rydon HN. 1977. Direct formation of peptide analogues of rubredoxin and four-iron ferredoxins from their components. JCS Chem Comm (24):908-909.
    • (1977) JCS Chem Comm , Issue.24 , pp. 908-909
    • Christou, G.1    Ridge, B.2    Rydon, H.N.3
  • 11
    • 0028818241 scopus 로고
    • Metal Search: A computer program that helps design tetrahedral metal-binding sites
    • Clarke ND, Yuan S-M. 1995. Metal Search: A computer program that helps design tetrahedral metal-binding sites. Proteins Struct Funct Genet 23:256-263.
    • (1995) Proteins Struct Funct Genet , vol.23 , pp. 256-263
    • Clarke, N.D.1    Yuan, S.-M.2
  • 12
    • 0030917147 scopus 로고    scopus 로고
    • The rational design and construction of a cuboidal iron-sulfur protein
    • Coldren CD, Hellinga HW, Caradonna JP. 1997. The rational design and construction of a cuboidal iron-sulfur protein. Proc Natl Acad Sci 94:6635-6640.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 6635-6640
    • Coldren, C.D.1    Hellinga, H.W.2    Caradonna, J.P.3
  • 14
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat BI, Mayo SL. 1997. De novo protein design: Fully automated sequence selection. Science 278:82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 16
    • 0027051883 scopus 로고
    • X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus
    • Day MW, Hsu BT, Joshua-Tor L, Park JB, Zhou ZH, Adams MWW, Rees DC. 1992. X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. Protein Sci 1:1494-1507.
    • (1992) Protein Sci , vol.1 , pp. 1494-1507
    • Day, M.W.1    Hsu, B.T.2    Joshua-Tor, L.3    Park, J.B.4    Zhou, Z.H.5    Adams, M.W.W.6    Rees, D.C.7
  • 18
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 19
    • 0002948271 scopus 로고
    • The iron-sulfur complex in rubredoxin
    • Spiro TG, eds. New York: Academic Press
    • Eaton WA, Lovenberg W. 1973. The iron-sulfur complex in rubredoxin. In: Spiro TG, eds. Iron-sulfur proteins, Vol. II. New York: Academic Press. pp 131-161.
    • (1973) Iron-sulfur Proteins , vol.2 , pp. 131-161
    • Eaton, W.A.1    Lovenberg, W.2
  • 20
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of Streptococcal protein G and comparison with NMR
    • Gallagher T, Alexander P, Bryan P, Gilliland GL. 1994. Two crystal structures of the B1 immunoglobulin-binding domain of Streptococcal protein G and comparison with NMR. Biochemistry 33:4721-4729.
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 24
    • 0029916620 scopus 로고    scopus 로고
    • Regulation of proteolytic activity by engineered tridentate metal binding loops
    • Halfon S, Craik CS. 1996. Regulation of proteolytic activity by engineered tridentate metal binding loops. J Am Chem Soc 118:1227-1228.
    • (1996) J Am Chem Soc , vol.118 , pp. 1227-1228
    • Halfon, S.1    Craik, C.S.2
  • 25
    • 0031885768 scopus 로고    scopus 로고
    • The construction of metal centers in proteins by rational design
    • Hellinga HW. 1998. The construction of metal centers in proteins by rational design. Folding Design 3:R1-R8.
    • (1998) Folding Design , vol.3
    • Hellinga, H.W.1
  • 26
    • 0026335211 scopus 로고
    • Construction of new ligand binding sites in proteins of known structure I. Computer-aided modeling of sites with predefined geometry
    • Hellinga HW, Richards FM. 1991. Construction of new ligand binding sites in proteins of known structure I. Computer-aided modeling of sites with predefined geometry. J Mol Biol 222:763-785.
    • (1991) J Mol Biol , vol.222 , pp. 763-785
    • Hellinga, H.W.1    Richards, F.M.2
  • 28
    • 17344363384 scopus 로고    scopus 로고
    • Solution structure of a α2D, a nativelike de novo designed protein
    • Hill BR, DeGrado WF. 1998. Solution structure of a α2D, a nativelike de novo designed protein. J Am Chem Soc 120:1138-1145.
    • (1998) J Am Chem Soc , vol.120 , pp. 1138-1145
    • Hill, B.R.1    Degrado, W.F.2
  • 29
    • 0028518514 scopus 로고
    • A designd peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues
    • Jackson DT, Burnnier J, Quan C, Stanely M, Tom J, Wells JA. 1994. A designd peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues. Science 266:243-247.
    • (1994) Science , vol.266 , pp. 243-247
    • Jackson, D.T.1    Burnnier, J.2    Quan, C.3    Stanely, M.4    Tom, J.5    Wells, J.A.6
  • 33
    • 0001505616 scopus 로고
    • Ligand variation and metal ion binding specificity in zinc finger peptides
    • Krizek BA, Merkle DL, Berg JM. 1993. Ligand variation and metal ion binding specificity in zinc finger peptides. Inorg Chem 32:937-940.
    • (1993) Inorg Chem , vol.32 , pp. 937-940
    • Krizek, B.A.1    Merkle, D.L.2    Berg, J.M.3
  • 34
    • 0024281294 scopus 로고
    • Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-binuclear iron cluster
    • LeGall J, Prickril I, Moura I, Xavier AV, Moura JJ, Huynh BH. 1988. Isolation and characterization of rubrerythrin, a non-heme iron protein from Desulfovibrio vulgaris that contains rubredoxin centers and a hemerythrin-binuclear iron cluster. Biochemistry 27:1636-1642.
    • (1988) Biochemistry , vol.27 , pp. 1636-1642
    • LeGall, J.1    Prickril, I.2    Moura, I.3    Xavier, A.V.4    Moura, J.J.5    Huynh, B.H.6
  • 36
    • 0028147533 scopus 로고
    • The crystal structure of a mutant protein with altered but improved hydrophobic core packing
    • Lim WA, Hodel A, Sauer RT, Richards FM. 1994. The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proc Natl Acad Sci USA 91:423-427.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 423-427
    • Lim, W.A.1    Hodel, A.2    Sauer, R.T.3    Richards, F.M.4
  • 37
    • 0013788501 scopus 로고
    • Rubredoxin: A new electron transfer protein from Clostridium pasteurianum
    • Lovenberg W, Sobel B. 1965. Rubredoxin: A new electron transfer protein from Clostridium pasteurianum. Proc Natl Acad Sci USA 54:193-199.
    • (1965) Proc Natl Acad Sci USA , vol.54 , pp. 193-199
    • Lovenberg, W.1    Sobel, B.2
  • 40
    • 0018569234 scopus 로고
    • Redox studies on rubredoxin from sulphate and sulfur reducing bacteria
    • Moura I, Moura JJG, Santos MH, Xavier AV, LeGall J. 1979. Redox studies on rubredoxin from sulphate and sulfur reducing bacteria. FEBS Lett 107:419-421.
    • (1979) FEBS Lett , vol.107 , pp. 419-421
    • Moura, I.1    Moura, J.J.G.2    Santos, M.H.3    Xavier, A.V.4    LeGall, J.5
  • 41
    • 0026091738 scopus 로고
    • Spectroscopic studies of cobalt and nickel substituted rubredoxin and desulforedoxin
    • Moura I, Teixeira M, LeGall J, Moura JJG. 1991. Spectroscopic studies of cobalt and nickel substituted rubredoxin and desulforedoxin. J Inorg Biochem 44: 127-139.
    • (1991) J Inorg Biochem , vol.44 , pp. 127-139
    • Moura, I.1    Teixeira, M.2    LeGall, J.3    Moura, J.J.G.4
  • 42
    • 0017844452 scopus 로고
    • A comparative spectroscopic study of two non-haem iron proteins lacking labile sulphide from Desulphovibrio gigas
    • Moura I, Xavier AV, Cammack R, Bruschi M, LeGall J. 1978. A comparative spectroscopic study of two non-haem iron proteins lacking labile sulphide from Desulphovibrio gigas. Biochim Biophys Acta 533:156-162.
    • (1978) Biochim Biophys Acta , vol.533 , pp. 156-162
    • Moura, I.1    Xavier, A.V.2    Cammack, R.3    Bruschi, M.4    LeGall, J.5
  • 43
    • 0038611543 scopus 로고
    • Cysteine-containing oligopeptide model complexes of iron-sulfur proteins
    • Sykes AG, ed. New York: Academic Press, Inc.
    • Nakamura A, Ueyama N. 1989. Cysteine-containing oligopeptide model complexes of iron-sulfur proteins. In: Sykes AG, ed. Advances in inorganic chemistry, Vol. 33. New York: Academic Press, Inc. pp 39-67.
    • (1989) Advances in Inorganic Chemistry , vol.33 , pp. 39-67
    • Nakamura, A.1    Ueyama, N.2
  • 44
    • 0013072368 scopus 로고
    • Isolation and characterization of rubredoxin and a two-(4Fe-4S) ferredoxin from Thermodesulfobacterium commune
    • Papavassiliou P, Hatchikian EC. 1985. Isolation and characterization of rubredoxin and a two-(4Fe-4S) ferredoxin from Thermodesulfobacterium commune. Biochim Biophys Acta 810:1-121.
    • (1985) Biochim Biophys Acta , vol.810 , pp. 1-121
    • Papavassiliou, P.1    Hatchikian, E.C.2
  • 46
    • 0015218714 scopus 로고
    • An analysis of the electron paramagnetic resonance spectrum of Pseudomonas oleovorans rubredoxin
    • Peisach J, Blumberg WE, Lode ET, Coon MJ. 1971. An analysis of the electron paramagnetic resonance spectrum of Pseudomonas oleovorans rubredoxin. J Biol Chem 246:5877-5881.
    • (1971) J Biol Chem , vol.246 , pp. 5877-5881
    • Peisach, J.1    Blumberg, W.E.2    Lode, E.T.3    Coon, M.J.4
  • 47
    • 0030978103 scopus 로고    scopus 로고
    • Construction of a catalytically active iron superoxide dismutase by rational protein design
    • Pinto AL, Hellinga HW, Caradonna JP. 1997. Construction of a catalytically active iron superoxide dismutase by rational protein design. Proc Natl Acad Sci USA 94:5562-5567.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5562-5567
    • Pinto, A.L.1    Hellinga, H.W.2    Caradonna, J.P.3
  • 48
    • 0043224256 scopus 로고    scopus 로고
    • Engineering cyclophilin into a proline-specific endopeptidase
    • Quénéneur E, Moutiez M, Charbonnier J-B. Ménez A. 1998. Engineering cyclophilin into a proline-specific endopeptidase. Nature 1998:301-304.
    • (1998) Nature , vol.1998 , pp. 301-304
    • Quénéneur, E.1    Moutiez, M.2    Charbonnier, J.-B.3    Ménez, A.4
  • 50
    • 0027289198 scopus 로고
    • The design of metal-binding sites in protein
    • Regan L. 1993. The design of metal-binding sites in protein. Ann Rev Biophys Biomol Struct 22:257-281.
    • (1993) Ann Rev Biophys Biomol Struct , vol.22 , pp. 257-281
    • Regan, L.1
  • 51
    • 0029016430 scopus 로고
    • Protein design: Novel metal-binding sites
    • Regan L. 1995. Protein design: Novel metal-binding sites. TIBS 20:280-285.
    • (1995) TIBS , vol.20 , pp. 280-285
    • Regan, L.1
  • 52
    • 0025644594 scopus 로고
    • The tetrahedral zinc(II)-binding site introduced into a designed protein
    • Regan L, Clarke ND. 1990. The tetrahedral zinc(II)-binding site introduced into a designed protein. Biochemistry 29:10878-10883.
    • (1990) Biochemistry , vol.29 , pp. 10878-10883
    • Regan, L.1    Clarke, N.D.2
  • 53
    • 0023812695 scopus 로고
    • Characterization of a helical protein designed from first principles
    • Regan L, DeGrado WF. 1988. Characterization of a helical protein designed from first principles. Science 241:976-978.
    • (1988) Science , vol.241 , pp. 976-978
    • Regan, L.1    DeGrado, W.F.2
  • 55
    • 0027686674 scopus 로고
    • Structure at 2.5 Å of a designed peptide that maintains solubility of membrane
    • Schafmeister CE, Miercke UW, Stroud RM. 1993. Structure at 2.5 Å of a designed peptide that maintains solubility of membrane. Protein Sci 262:734-738.
    • (1993) Protein Sci , vol.262 , pp. 734-738
    • Schafmeister, C.E.1    Miercke, U.W.2    Stroud, R.M.3
  • 56
    • 0031055169 scopus 로고    scopus 로고
    • x cluster in the photosystem I reaction center
    • x cluster in the photosystem I reaction center. Protein Sci 6:340-346.
    • (1997) Protein Sci , vol.6 , pp. 340-346
    • Scott, M.P.1    Biggins, J.2
  • 57
    • 0001117058 scopus 로고    scopus 로고
    • The construction and design of beta sheets
    • Smith CK, Regan L. 1997. The construction and design of beta sheets. Acc Chem Res 30:153-161.
    • (1997) Acc Chem Res , vol.30 , pp. 153-161
    • Smith, C.K.1    Regan, L.2
  • 58
    • 0028175780 scopus 로고    scopus 로고
    • A thermodynamic scale for the β-sheet forming tendencies of the amino acids
    • Smith CK, Withka JM, Regan L. 1996. A thermodynamic scale for the β-sheet forming tendencies of the amino acids. Biochemistry 33:5510-5517.
    • (1996) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 59
    • 0001531848 scopus 로고    scopus 로고
    • Protein control of redox potentials of iron-sulfur proteins
    • Stephens PJ, Jollie DR, Warshel A. 1996. Protein control of redox potentials of iron-sulfur proteins. Chem Rev 96:2491-2513.
    • (1996) Chem Rev , vol.96 , pp. 2491-2513
    • Stephens, P.J.1    Jollie, D.R.2    Warshel, A.3
  • 61
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modelling and drug design program
    • Vriend G. 1990. WHAT IF: A molecular modelling and drug design program. J Mol Graph 8:52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 62
    • 0018782265 scopus 로고
    • The structure of rubredoxin at 1.2 Å resolution
    • Watenpaugh KD, Sieker LC, Jensen LH. 1979. The structure of rubredoxin at 1.2 Å resolution. J Mol Biol 131:509-522.
    • (1979) J Mol Biol , vol.131 , pp. 509-522
    • Watenpaugh, K.D.1    Sieker, L.C.2    Jensen, L.H.3
  • 63
    • 0019325181 scopus 로고
    • Crystallographic refinement of rubredoxin at 1.2 Å resolution
    • Watenpaugh KD, Sieker LC, Jensen LH. 1980. Crystallographic refinement of rubredoxin at 1.2 Å resolution. J Mol Biol 138:615-633.
    • (1980) J Mol Biol , vol.138 , pp. 615-633
    • Watenpaugh, K.D.1    Sieker, L.C.2    Jensen, L.H.3
  • 64
    • 0028309466 scopus 로고
    • Engineering of betabellin 14D: Disulfide-induced folding of a β-sheet protein
    • Yan Y, Erickson BW. 1994. Engineering of betabellin 14D: Disulfide-induced folding of a β-sheet protein. Protein Sci 3:1069-1073.
    • (1994) Protein Sci , vol.3 , pp. 1069-1073
    • Yan, Y.1    Erickson, B.W.2
  • 65
    • 0028998016 scopus 로고
    • Molecular dynamics simulations of rubredoxin from Clostridium pasteurianum: Changes in structure and electrostatic potential during redox reactions
    • Yelle RB, Park N-S, Ichiye T. 1995. Molecular dynamics simulations of rubredoxin from Clostridium pasteurianum: Changes in structure and electrostatic potential during redox reactions. Proteins Struct Funct Genet 22:154-167.
    • (1995) Proteins Struct Funct Genet , vol.22 , pp. 154-167
    • Yelle, R.B.1    Park, N.-S.2    Ichiye, T.3


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