메뉴 건너뛰기




Volumn 5, Issue 8, 1997, Pages 1077-1092

Binding of allosteric effectors to ribonucleotide reductase protein R1: Reduction of active-site cysteines promotes substrate binding

Author keywords

Allosteric effectors; Nucleotide binding; Radical transfer; Reduced active site; Ribonucleotide reductase

Indexed keywords


EID: 0031571616     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00259-1     Document Type: Article
Times cited : (234)

References (65)
  • 1
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • Reichard, P. (1993). From RNA to DNA, why so many ribonucleotide reductases? Science 260, 1773-1777.
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 2
    • 0025293287 scopus 로고
    • Three-dimensional structure of the free radical protein of ribonucleotide reductase
    • Nordlund, P., Sjöberg, B.-M. & Eklund, H. (1990). Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345, 593-598.
    • (1990) Nature , vol.345 , pp. 593-598
    • Nordlund, P.1    Sjöberg, B.-M.2    Eklund, H.3
  • 3
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin, U. & Eklund, H. (1994). Structure of ribonucleotide reductase protein R1. Nature 370, 533-539.
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 4
    • 0030603925 scopus 로고    scopus 로고
    • The ten-stranded β/α barrel in ribonucleotide reductase protein R1
    • Uhlin, U. & Eklund, H. (1996). The ten-stranded β/α barrel in ribonucleotide reductase protein R1. J. MoIl Biol. 262, 358-369.
    • (1996) J. MoIl Biol. , vol.262 , pp. 358-369
    • Uhlin, U.1    Eklund, H.2
  • 5
    • 0023643435 scopus 로고
    • Location of the redoxactive thiols of ribonucleotide reductase: Sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes
    • Lin, A.-N.I., Ashley, G.W. & Stubbe, J. (1987). Location of the redoxactive thiols of ribonucleotide reductase: Sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes. Biochemistry 26, 6905-6909.
    • (1987) Biochemistry , vol.26 , pp. 6905-6909
    • Lin, A.-N.I.1    Ashley, G.W.2    Stubbe, J.3
  • 6
    • 0024349130 scopus 로고
    • Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli
    • Åberg, A., et al., Sjöberg, B.-M. (1989). Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli. J. Biol. Chem. 264, 12249-1 2252.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12249-12252
    • Åberg, A.1    Sjöberg, B.-M.2
  • 7
    • 0026801085 scopus 로고
    • A model for the role of multiple cysteine residues involved in ribonucleotide reduction: Amazing and still confusing
    • Mao, S.S., et al., & Stubbe, J. (1992). A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing. Biochemistry 31, 9733-9743.
    • (1992) Biochemistry , vol.31 , pp. 9733-9743
    • Mao, S.S.1    Stubbe, J.2
  • 8
    • 0026788358 scopus 로고
    • Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: Evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity
    • Mao, S.S., Yu, G.X., Chalfoun, D. & Stubbe, J. (1992). Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity. Biochemistry 31, 9752-9759.
    • (1992) Biochemistry , vol.31 , pp. 9752-9759
    • Mao, S.S.1    Yu, G.X.2    Chalfoun, D.3    Stubbe, J.4
  • 9
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • Licht, S., Gerfen, G.J. & Stubbe, J. (1996). Thiyl radicals in ribonucleotide reductases. Science 271, 477-481.
    • (1996) Science , vol.271 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 10
    • 0014694297 scopus 로고
    • Role of effector binding in allosteric control of ribonucleoside diphosphate reductase
    • Brown, N.C. & Reichard, P. (1969). Role of effector binding in allosteric control of ribonucleoside diphosphate reductase. J. Mol. Biol. 46, 39-55.
    • (1969) J. Mol. Biol. , vol.46 , pp. 39-55
    • Brown, N.C.1    Reichard, P.2
  • 11
    • 0023655439 scopus 로고
    • Deoxyribonucleoside-triphosphate imbalance death: Deoxyadenosine-induced dNTP imbalance and DNA double strand breaks in mouse FM3A cells and the mechanism of cell death
    • Yoshioka, A., Tanaka, S., Hiraoka, O., Koyama, Y., Hirota, Y. & Wataya, Y. (1987). Deoxyribonucleoside-triphosphate imbalance death: deoxyadenosine-induced dNTP imbalance and DNA double strand breaks in mouse FM3A cells and the mechanism of cell death. Biochem. Biophys. Res. Commun. 146, 258-264.
    • (1987) Biochem. Biophys. Res. Commun. , vol.146 , pp. 258-264
    • Yoshioka, A.1    Tanaka, S.2    Hiraoka, O.3    Koyama, Y.4    Hirota, Y.5    Wataya, Y.6
  • 12
    • 0023746738 scopus 로고
    • Mutagenesis and deoxyribonucleotide pool imbalance
    • Kunz, B.A. (1988). Mutagenesis and deoxyribonucleotide pool imbalance. Mutat. Res. 200, 133-147.
    • (1988) Mutat. Res. , vol.200 , pp. 133-147
    • Kunz, B.A.1
  • 13
    • 0021253747 scopus 로고
    • The genetic consequences of nucleotide precursor pool imbalance in mammalian cells
    • Meuth, M. (1984). The genetic consequences of nucleotide precursor pool imbalance in mammalian cells. Mutat. Res. 126, 107-112
    • (1984) Mutat. Res. , vol.126 , pp. 107-112
    • Meuth, M.1
  • 14
    • 0024505072 scopus 로고
    • The molecular basis of mutations induced by deoxyribonucleoside triphosphate pool imbalances in mammalian cells
    • Meuth, M. (1989). The molecular basis of mutations induced by deoxyribonucleoside triphosphate pool imbalances in mammalian cells. Exp. Cell. Res. 181, 305-316.
    • (1989) Exp. Cell. Res. , vol.181 , pp. 305-316
    • Meuth, M.1
  • 15
    • 0023881789 scopus 로고
    • Molecular cloning of the cDNA for a mutant mouse ribonucleotide reductase M1 that produces a dominant mutator phenotype in mammalian cells
    • Caras, LW. & Martin, D.W., Jr. (1988). Molecular cloning of the cDNA for a mutant mouse ribonucleotide reductase M1 that produces a dominant mutator phenotype in mammalian cells. Mol. Cell. Biol. 8, 2698-2704.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2698-2704
    • Caras, L.W.1    Martin Jr., D.W.2
  • 16
    • 0023024469 scopus 로고
    • A photoaffinity-labeled allosteric site in Escherichia coli ribonucleotide reductase
    • Eriksson, S., Sjöberg, B.-M., Jörnvall, H. & Carlquist, M. (1986). A photoaffinity-labeled allosteric site in Escherichia coli ribonucleotide reductase. J. Biol. Chem. 261, 1878-1882.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1878-1882
    • Eriksson, S.1    Sjöberg, B.-M.2    Jörnvall, H.3    Carlquist, M.4
  • 17
    • 0029896950 scopus 로고    scopus 로고
    • A kinetic study on the influence of nucleoside triphosphate effectors on subunit interaction in mouse ribonucleotide reductase
    • Ingemarson, R. & Thelander, L. (1996). A kinetic study on the influence of nucleoside triphosphate effectors on subunit interaction in mouse ribonucleotide reductase. Biochemistry 35, 8603-8609.
    • (1996) Biochemistry , vol.35 , pp. 8603-8609
    • Ingemarson, R.1    Thelander, L.2
  • 19
    • 0029812067 scopus 로고    scopus 로고
    • Two conserved tyrosine residues in protein R1 are most likely a part of an electron transfer chain in ribonucleotide reductase from E. coli
    • Ekberg, M., Sahlin, M., Eriksson, M. & Sjöberg, B.-M. (1996). Two conserved tyrosine residues in protein R1 are most likely a part of an electron transfer chain in ribonucleotide reductase from E. coli. J. Biol. Chem. 271, 20655-20659.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20655-20659
    • Ekberg, M.1    Sahlin, M.2    Eriksson, M.3    Sjöberg, B.-M.4
  • 20
    • 0029657918 scopus 로고    scopus 로고
    • The Cys292→Ala substitution in protein R1 of class I ribonucleotide reductase from Escherichia coli has a global effect on nucleotide binding at the specificity-determining allosteric site
    • Ormö, M. & Sjöberg, B-M. (1996). The Cys292→Ala substitution in protein R1 of class I ribonucleotide reductase from Escherichia coli has a global effect on nucleotide binding at the specificity-determining allosteric site. Eur. J. Biochem. 241, 363-367.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 363-367
    • Ormö, M.1    Sjöberg, B.-M.2
  • 21
    • 0018882304 scopus 로고
    • Pyridine nucleotide - Disulfide oxidoreductases
    • (Jeffery, J., ed), Birkhöuser, Basel
    • Holmgren, A. (1980). Pyridine nucleotide - disulfide oxidoreductases. In Dehydrogenases Requiring Nicotinamide Coenzymes. (Jeffery, J., ed), pp. 149-180, Birkhöuser, Basel.
    • (1980) Dehydrogenases Requiring Nicotinamide Coenzymes , pp. 149-180
    • Holmgren, A.1
  • 22
    • 0000324547 scopus 로고
    • Variations on a theme: The family of FAD-dependent NAD(P)H-(disulphide)-oxidoreductases
    • Pai, E.F. (1991). Variations on a theme: the family of FAD-dependent NAD(P)H-(disulphide)-oxidoreductases. Curr. Opin. Struct. Biol. 1, 796-803.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 796-803
    • Pai, E.F.1
  • 23
    • 0024959343 scopus 로고
    • A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution
    • Karplus, P.A., Pai, E.F. & Schulz, G.E. (1989). A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution. Eur. J. Biochem. 178, 693-703.
    • (1989) Eur. J. Biochem. , vol.178 , pp. 693-703
    • Karplus, P.A.1    Pai, E.F.2    Schulz, G.E.3
  • 24
    • 0027050496 scopus 로고
    • NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins
    • Xia, T.-H., et al., & Wüthrich, K. (1992). NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. Protein Sci. 1, 310-321.
    • (1992) Protein Sci. , vol.1 , pp. 310-321
    • Xia, T.-H.1    Wüthrich, K.2
  • 25
    • 0028773644 scopus 로고
    • The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin
    • Qin, J., Clore, G.M. & Gronenborn, A.M. (1994). The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure 2, 503-522.
    • (1994) Structure , vol.2 , pp. 503-522
    • Qin, J.1    Clore, G.M.2    Gronenborn, A.M.3
  • 26
    • 0028774178 scopus 로고
    • High-resolution structures of oxidized and reduced Escherichia coli thioredoxin
    • Jeng, M.-F., et al., & Dyson, H.J. (1994). High-resolution structures of oxidized and reduced Escherichia coli thioredoxin. Structure 2, 853-868.
    • (1994) Structure , vol.2 , pp. 853-868
    • Jeng, M.-F.1    Dyson, H.J.2
  • 27
    • 0028220312 scopus 로고
    • Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution
    • Waksman, G., Krishna, T.S.R., Williams, C.H., Jr. & Kuriyan, J. (1994). Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. J. Mol. Biol. 236, 800-816.
    • (1994) J. Mol. Biol. , vol.236 , pp. 800-816
    • Waksman, G.1    Krishna, T.S.R.2    Williams Jr., C.H.3    Kuriyan, J.4
  • 28
    • 0029159834 scopus 로고
    • The structure of a reduced mutant T4 glutaredoxin
    • Ingelman, M., Nordlund, P. & Eklund, H. (1995). The structure of a reduced mutant T4 glutaredoxin. FEBS Lett. 370, 209-211.
    • (1995) FEBS Lett. , vol.370 , pp. 209-211
    • Ingelman, M.1    Nordlund, P.2    Eklund, H.3
  • 29
    • 0026652152 scopus 로고
    • Site directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2
    • Climent, L, Sjöberg, B.-M. & Huang, C.Y. (1992). Site directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Biochemistry 31, 4801-4807.
    • (1992) Biochemistry , vol.31 , pp. 4801-4807
    • Climent, L.1    Sjöberg, B.-M.2    Huang, C.Y.3
  • 30
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • Nordlund, P. & Eklund, H. (1993). Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J. Mol. Biol. 232, 123-164.
    • (1993) J. Mol. Biol. , vol.232 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 31
    • 0028774182 scopus 로고
    • The ribonucleotide reductase jigsaw puzzle: A large piece falls into place
    • Sjöberg, B.M. (1994). The ribonucleotide reductase jigsaw puzzle: a large piece falls into place. Structure 2, 793-796.
    • (1994) Structure , vol.2 , pp. 793-796
    • Sjöberg, B.M.1
  • 32
    • 0028963767 scopus 로고
    • Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase
    • Rova, U., Goodtzova, K., Ingemarson, R., Behravan, G., Gröslund, A. & Thelander, L. (1995). Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase. Biochemistry 34, 4267-4275.
    • (1995) Biochemistry , vol.34 , pp. 4267-4275
    • Rova, U.1    Goodtzova, K.2    Ingemarson, R.3    Behravan, G.4    Gröslund, A.5    Thelander, L.6
  • 33
    • 0017239363 scopus 로고
    • Active site of ribonucleoside diphosphate reductase from Escherichia coli. Inactivation of the enzyme by 2′substituted ribonucleoside diphosphates
    • Thelander, L., Larsson, B., Hobbs, J. & Eckstein, F. (1976). Active site of ribonucleoside diphosphate reductase from Escherichia coli. Inactivation of the enzyme by 2′substituted ribonucleoside diphosphates. J. Biol. Chem. 251, 1398-1405.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1398-1405
    • Thelander, L.1    Larsson, B.2    Hobbs, J.3    Eckstein, F.4
  • 34
    • 0021099682 scopus 로고
    • A substrate radical intermediate in the reaction between ribonucleotide reductase from Escherichia coli and 2′-azido-2′-deoxy nucleoside diphosphates
    • Sjöberg, B.-M., Gräslund, A. & Eckstein, F. (1983). A substrate radical intermediate in the reaction between ribonucleotide reductase from Escherichia coli and 2′-azido-2′-deoxy nucleoside diphosphates. J. Biol. Chem. 258, 8060-8067.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8060-8067
    • Sjöberg, B.-M.1    Gräslund, A.2    Eckstein, F.3
  • 35
    • 8944260410 scopus 로고    scopus 로고
    • Inactivation of Escherichia coli ribonucleotide reductase by 2′-deoxy-2′-mercaptouridine 5′-diphosphate. Electron paramagnetic resonance evidence for a transient protein perthiyl radical
    • Coves, J., Defallois, L.L.H., Lepape, L., Decout, J.L. & Fontecave, M. (1996). Inactivation of Escherichia coli ribonucleotide reductase by 2′-deoxy-2′-mercaptouridine 5′-diphosphate. Electron paramagnetic resonance evidence for a transient protein perthiyl radical. Biochemistry 35, 8595-8602.
    • (1996) Biochemistry , vol.35 , pp. 8595-8602
    • Coves, J.1    Defallois, L.L.H.2    Lepape, L.3    Decout, J.L.4    Fontecave, M.5
  • 36
    • 0029146607 scopus 로고
    • EPR investigations of the inactivation of E. coli ribonucleotide reductase with 2′-azido-2′-deoxyuridine 5′-diphosphate: Evidence for the involvement of the thiyl radical of C225-R1
    • van der Donk, W.A., Stubbe, J., Gerfen, G.J., Beilew, B.F. & Griffin, R.G. (1995). EPR investigations of the inactivation of E. coli ribonucleotide reductase with 2′-azido-2′-deoxyuridine 5′-diphosphate: evidence for the involvement of the thiyl radical of C225-R1. J. Am. Chem. Soc. 117, 8908-8916.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8908-8916
    • Van Der Donk, W.A.1    Stubbe, J.2    Gerfen, G.J.3    Beilew, B.F.4    Griffin, R.G.5
  • 37
    • 0030036601 scopus 로고    scopus 로고
    • Inactivation of ribonucleotide reductase by (E)2′-fluoromethylene-2′-deoxycytidine 5′-diphosphate: A paradigm for nucleotide mechanism-based
    • van der Donk., W.A., Yu, G.X., Silva, D.J. & Stubbe, J. (1996). Inactivation of ribonucleotide reductase by (E)2′-fluoromethylene-2′-deoxycytidine 5′-diphosphate: a paradigm for nucleotide mechanism-based. Biochemistry 35, 8381-8391.
    • (1996) Biochemistry , vol.35 , pp. 8381-8391
    • Van Der Donk, W.A.1    Yu, G.X.2    Silva, D.J.3    Stubbe, J.4
  • 38
    • 0026786291 scopus 로고
    • Interaction of C225SR1 mutant subunit of ribonucleotide reductase with R2 and nucleoside diphosphates: Tales of a suicidal enzyme
    • Mao, S.S., Holler, T.P., Bollinger, J.M., Jr., Yu, G.X., Johnston, M.I. & Stubbe, J. (1992). Interaction of C225SR1 mutant subunit of ribonucleotide reductase with R2 and nucleoside diphosphates: tales of a suicidal enzyme. Biochemistry 31, 9744-9751.
    • (1992) Biochemistry , vol.31 , pp. 9744-9751
    • Mao, S.S.1    Holler, T.P.2    Bollinger Jr., J.M.3    Yu, G.X.4    Johnston, M.I.5    Stubbe, J.6
  • 39
    • 0029743073 scopus 로고    scopus 로고
    • Identification of an active site residue of the R1 subunit of ribonucleotide reductase from Escherichia coli: Characterization of substrate-induced polypeptide cleavage by C225SR1
    • van der Donk, W.A., Zeng, C., Biemann, K., Stubbe, J. (1996). Identification of an active site residue of the R1 subunit of ribonucleotide reductase from Escherichia coli: characterization of substrate-induced polypeptide cleavage by C225SR1. Biochemistry 35, 10058-10067.
    • (1996) Biochemistry , vol.35 , pp. 10058-10067
    • Van Der Donk, W.A.1    Zeng, C.2    Biemann, K.3    Stubbe, J.4
  • 40
    • 0022339341 scopus 로고
    • Mechanism of inactivation of Escherichia coli ribonucleotide reductase by 2′-chloro-2-deoxyuridine 5′-diphosphate: Evidence for generation of a 2′-deoxy-3′-ketonucleotide via a net 1,2 hydrogen shift
    • Ator, M.A. & Stubbe, J. (1985). Mechanism of inactivation of Escherichia coli ribonucleotide reductase by 2′-chloro-2-deoxyuridine 5′-diphosphate: evidence for generation of a 2′-deoxy-3′-ketonucleotide via a net 1,2 hydrogen shift. Biochemistry 24, 7214-7221.
    • (1985) Biochemistry , vol.24 , pp. 7214-7221
    • Ator, M.A.1    Stubbe, J.2
  • 41
    • 0017669982 scopus 로고
    • Ribonucleotide reductase from Escherichia coli. Identification of allosteric effector sites by chromatography on immobilized effectors
    • von Döbeln, U. (1977). Ribonucleotide reductase from Escherichia coli. Identification of allosteric effector sites by chromatography on immobilized effectors. Biochemistry 16, 4368-4371.
    • (1977) Biochemistry , vol.16 , pp. 4368-4371
    • Von Döbeln, U.1
  • 42
    • 0025091418 scopus 로고
    • An ultrafiltration assay for nucleotide binding to ribonucleotide reductase
    • Ormö, M. & Sjöberg, B.-M. (1990). An ultrafiltration assay for nucleotide binding to ribonucleotide reductase. Anal. Biochem. 189, 138-141.
    • (1990) Anal. Biochem. , vol.189 , pp. 138-141
    • Ormö, M.1    Sjöberg, B.-M.2
  • 43
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • Lambright, D.G., Noel, J.P., Hamm, H.E. & Sigler, P.B. (1994). Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 369, 621-628.
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 44
    • 0029974121 scopus 로고    scopus 로고
    • Allosteric regulation of the third ribonucleotide reductase (NrdEF enzyme) from enterobacteriaceae
    • Eliasson, R., Pontis, E., Jordan, A. & Reichard, P. (1996). Allosteric regulation of the third ribonucleotide reductase (NrdEF enzyme) from enterobacteriaceae. J. Biol. Chem. 271, 26582-26587.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26582-26587
    • Eliasson, R.1    Pontis, E.2    Jordan, A.3    Reichard, P.4
  • 45
    • 0021693466 scopus 로고
    • Overproduction of the B1 subunit of ribonucleotide reductase with gene amplification
    • Larsson, A. (1984). Overproduction of the B1 subunit of ribonucleotide reductase with gene amplification. Acta Chem. Scand. B 38, 905-907.
    • (1984) Acta Chem. Scand. B , vol.38 , pp. 905-907
    • Larsson, A.1
  • 46
    • 0023024912 scopus 로고
    • Overproduction and purification of the B2 subunit of ribonucleotide reductase from Escherichia coli
    • Sjöberg, B-M., Hahne, S., Karlsson, M., Jörnvall, H., Göransson, M. & Uhlin, B.E. (1986). Overproduction and purification of the B2 subunit of ribonucleotide reductase from Escherichia coli. J. Biol. Chem. 261, 5658-5662.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5658-5662
    • Sjöberg, B.-M.1    Hahne, S.2    Karlsson, M.3    Jörnvall, H.4    Göransson, M.5    Uhlin, B.E.6
  • 47
    • 0024297296 scopus 로고
    • Radical formation in the dimeric small subunit of ribonucleotide reductase requires only one tyrosine 122
    • Larsson, Å., Karlsson, M., Sahlin, M. & Sjöberg, B.-M. (1988). Radical formation in the dimeric small subunit of ribonucleotide reductase requires only one tyrosine 122. J. Biol. Chem. 263, 17780-17784.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17780-17784
    • Larsson, Å.1    Karlsson, M.2    Sahlin, M.3    Sjöberg, B.-M.4
  • 48
    • 0027493255 scopus 로고
    • Crystallization and crystallographic investigations of ribonucleotide reductase protein R1 from Escherichia coli
    • Uhlin, U., Uhlin, T. & Eklund, H. (1993). Crystallization and crystallographic investigations of ribonucleotide reductase protein R1 from Escherichia coli. FEBS Lett. 336, 148-152.
    • (1993) FEBS Lett. , vol.336 , pp. 148-152
    • Uhlin, U.1    Uhlin, T.2    Eklund, H.3
  • 49
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • (Sawyer, L., Isaacs, N. & Bailey, S., eds.), SERC Daresbury Laboratory, England
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds.), pp. 56-62, SERC Daresbury Laboratory, England.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 50
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 51
    • 84913050729 scopus 로고
    • An efficient general-purpose least-squares refinement program for macromolecular structures
    • Tronrud, D.E., Ten Eyck, L.F. & Matthews, B.W. (1987). An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Cryst. A 43, 489-501.
    • (1987) Acta Cryst. A , vol.43 , pp. 489-501
    • Tronrud, D.E.1    Ten Eyck, L.F.2    Matthews, B.W.3
  • 52
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 53
    • 84944812409 scopus 로고
    • Improved fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. (1986). Improved fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
    • (1986) Acta Cryst. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 54
    • 0002552477 scopus 로고
    • A, yaap, asap, @#*? A set of averaging programs
    • (Dodson, E/J., Cover, S. & Wolf, W., eds), SERC Daresbury Laboratory, Warrington, UK
    • Jones, T.A. (1992). A, yaap, asap, @#*? A set of averaging programs. In Molecular Replacement (Dodson, E/J., Cover, S. & Wolf, W., eds), pp. 91-105, SERC Daresbury Laboratory, Warrington, UK.
    • (1992) Molecular Replacement , pp. 91-105
    • Jones, T.A.1
  • 56
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, T.A., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, T.A.1    Kuriyan, J.2    Karplus, M.3
  • 58
    • 0027399487 scopus 로고
    • Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: Implications for ATCase mutants and the mechanism of negative cooperativity
    • Kosman, R.P., Gouaux, J.E. & Lipscomb, W.N. (1993). Crystal structure of CTP-ligated T state aspartate transcarbamoylase at 2.5 A resolution: implications for ATCase mutants and the mechanism of negative cooperativity. Proteins 15, 147-1 76.
    • (1993) Proteins , vol.15 , pp. 147-176
    • Kosman, R.P.1    Gouaux, J.E.2    Lipscomb, W.N.3
  • 60
    • 0028913538 scopus 로고
    • Crystal structure of casein kinase-1, a phosphate-directed protein kinase
    • Xu, R.M., Carmel, G., Sweet, R.M., Kuret, J. & Cheng, X. (1995). Crystal structure of casein kinase-1, a phosphate-directed protein kinase. EMBO J. 14, 101 5-1023.
    • (1995) EMBO J. , vol.14 , pp. 1015-1023
    • Xu, R.M.1    Carmel, G.2    Sweet, R.M.3    Kuret, J.4    Cheng, X.5
  • 61
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (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.1
  • 62
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 64
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graph. 6, 219-220.
    • (1988) J. Mol. Graph. , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 65
    • 0028057108 scopus 로고
    • Raster3D version 2.0 - A program for photorealistic molecular graphics
    • Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D version 2.0 - a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.
    • (1994) Acta Cryst. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.