메뉴 건너뛰기




Volumn 48, Issue 22, 2009, Pages 4988-4998

Flexibility in the inducer binding region is crucial for allostery in the Escherichia coli lactose repressor

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC MECHANISMS; ALLOSTERIC TRANSITION; ALLOSTERY; BINDING AFFINITIES; BOUND STATE; CELL EXTRACTS; CONFORMATIONAL CHANGE; DISULFIDE BONDS; DOUBLE MUTANTS; INTER-RESIDUE HYDROGEN BONDS; KINETIC CONSTANT; OXIDIZED STATE; PARALLEL CHANGES; REDUCED-STATE; SIDE CHAINS; SINGLE MUTANT; SPATIAL RELATIONSHIPS; TARGETED MOLECULAR DYNAMICS; WILD TYPES; WILD-TYPE PROTEINS;

EID: 66649102153     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9002343     Document Type: Article
Times cited : (20)

References (38)
  • 1
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey, N. M., and Benkovic, S. J. (2008) Allosteric regulation and catalysis emerge via a common route. Nat. Chem. Biol. 4, 474-482.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 3
    • 54249116230 scopus 로고
    • Genetic regulatory mechanisms in the synthesis of proteins
    • Jacob, F., and Monod, J. (1961) Genetic regulatory mechanisms in the synthesis of proteins. J. Mol. Biol. 3, 318-356.
    • (1961) J. Mol. Biol. , vol.3 , pp. 318-356
    • Jacob, F.1    Monod, J.2
  • 4
    • 0031961672 scopus 로고    scopus 로고
    • Lactose repressor protein: Functional properties and structure
    • Matthews, K. S., and Nichols, J. C. (1998) Lactose repressor protein: Functional properties and structure. Prog. Nucleic Acid Res. Mol. Biol. 58, 127-164.
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.58 , pp. 127-164
    • Matthews, K.S.1    Nichols, J.C.2
  • 6
    • 0027426159 scopus 로고
    • Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics
    • Chuprina, V. P., Rullmann, J. A. C., Lamerichs, R. M. J. N., van Boom, J. H., Boelens, R., and Kaptein, R. (1993) Structure of the complex of lac repressor headpiece and an 11 base-pair half-operator determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. J. Mol. Biol. 234, 446-462.
    • (1993) J. Mol. Biol. , vol.234 , pp. 446-462
    • Chuprina, V.P.1    Rullmann, J.A.C.2    Lamerichs, R.M.J.N.3    Van Boom, J.H.4    Boelens, R.5    Kaptein, R.6
  • 7
    • 0029004903 scopus 로고
    • Crystal structure of lac repressor core tetramer and its implications for DNA looping
    • Friedman, A. M., Fischmann, T. O., and Steitz, T. A. (1995) Crystal structure of lac repressor core tetramer and its implications for DNA looping. Science 268, 1721-1727.
    • (1995) Science , vol.268 , pp. 1721-1727
    • Friedman, A.M.1    Fischmann, T.O.2    Steitz, T.A.3
  • 8
    • 0029938053 scopus 로고    scopus 로고
    • Crystal structure of the lactose operon repressor and its complexes with DNA and inducer
    • Lewis, M., Chang, G., Horton, N. C., Kercher, M. A., Pace, H. C., Schumacher, M. A., Brennan, R. G., and Lu, P. (1996) Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Science 271, 1247-1254. (Pubitemid 26082644)
    • (1996) Science , vol.271 , Issue.5253 , pp. 1247-1254
    • Lewis, M.1    Chang, G.2    Horton, N.C.3    Kercher, M.A.4    Pace, H.C.5    Schumacher, M.A.6    Brennan, R.G.7    Lu, P.8
  • 9
    • 0026723976 scopus 로고
    • Deletion of lactose repressor carboxyl-terminal domain affects tetramer formation
    • Chen, J., and Matthews, K. S. (1992) Deletion of lactose repressor carboxyl-terminal domain affects tetramer formation. J. Biol. Chem. 267, 13843-13850.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13843-13850
    • Chen, J.1    Matthews, K.S.2
  • 10
    • 53149104770 scopus 로고    scopus 로고
    • The Venus flytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors
    • Felder, C. B., Graul, R. C., Lee, A. Y., Merkle, H. P., and Sadee, W. (1999) The Venus flytrap of periplasmic binding proteins: An ancient protein module present in multiple drug receptors. AAPS J. 1, 7-26.
    • (1999) AAPS J. , vol.1 , pp. 7-26
    • Felder, C.B.1    Graul, R.C.2    Lee, A.Y.3    Merkle, H.P.4    Sadee, W.5
  • 11
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F. A., and Ledvina, P. S. (1996) Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes. Mol. Microbiol. 20, 17-25.
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 12
    • 20344362178 scopus 로고    scopus 로고
    • Amino acid recognition by venus flytrap domains is encoded in an 8-residue motif
    • DOI 10.1002/bip.20229
    • Acher, F. C., and Bertrand, H. O. (2005) Amino acid recognition by Venus flytrap domains is encoded in an 8-residue motif. Biopolymers 80, 357-366. (Pubitemid 40791066)
    • (2005) Biopolymers - Peptide Science Section , vol.80 , Issue.2-3 , pp. 357-366
    • Acher, F.C.1    Bertrand, H.-O.2
  • 13
    • 0018355613 scopus 로고
    • Genetic studies of the lac repressor XI. On aspects of lac repressor structure suggested by genetic experiments
    • Miller, J. H. (1979) Genetic studies of the lac repressor XI. On aspects of lac repressor structure suggested by genetic experiments. J. Mol. Biol. 131, 249-258.
    • (1979) J. Mol. Biol. , vol.131 , pp. 249-258
    • Miller, J.H.1
  • 14
    • 2342519701 scopus 로고    scopus 로고
    • Genetic studies of the Lac repressor XV: 4000 Single amino acid substitutions and analysis of the resulting phenotypes on the basis of the protein structure
    • Suckow, J., Markiewicz, P., Kleina, L. G., Miller, J., Kisters-Woike, B., and Müller-Hill, B. (1996) Genetic studies of the Lac repressor XV: 4000 single amino acid substitutions and analysis of the resulting phenotypes on the basis of the protein structure. J. Mol. Biol. 261, 509-523.
    • (1996) J. Mol. Biol. , vol.261 , pp. 509-523
    • Suckow, J.1    Markiewicz, P.2    Kleina, L.G.3    Miller, J.4    Kisters-Woike, B.5    Müller-Hill, B.6
  • 16
    • 0034089394 scopus 로고    scopus 로고
    • A closer view of the conformation of the Lac repressor bound to operator
    • Bell, C. E., and Lewis, M. (2000) A closer view of the conformation of the Lac repressor bound to operator. Nat. Struct. Biol. 7, 209-214.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 209-214
    • Bell, C.E.1    Lewis, M.2
  • 18
    • 0142179045 scopus 로고    scopus 로고
    • Allosteric transition pathways in the lactose repressor protein core domains: Asymmetric motions in a homodimer
    • DOI 10.1110/ps.03188303
    • Flynn, T. C., Swint-Kruse, L., Kong, Y., Booth, C., Matthews, K. S., and Ma, J. (2003) Allosteric transition pathways in the lactose repressor protein core domains: Asymmetric motions in a homodimer. Protein Sci. 12, 2523-2541. (Pubitemid 37310792)
    • (2003) Protein Science , vol.12 , Issue.11 , pp. 2523-2541
    • Flynn, T.C.1    Swint-Kruse, L.2    Kong, Y.3    Booth, C.4    Matthews, K.S.5    Ma, J.6
  • 19
    • 0033987659 scopus 로고    scopus 로고
    • Generation of an AraC-araBAD promoter-regulated T7 expression system
    • Wycuff, D. R., and Matthews, K. S. (2000) Generation of an AraC-araBAD promoter-regulated T7 expression system. Anal. Biochem. 277, 67-73.
    • (2000) Anal. Biochem. , vol.277 , pp. 67-73
    • Wycuff, D.R.1    Matthews, K.S.2
  • 20
    • 0032718889 scopus 로고    scopus 로고
    • Glycine insertion in the hinge region of lactose repressor protein alters DNA binding
    • Falcon, C. M., and Matthews, K. S. (1999) Glycine insertion in the hinge region of lactose repressor protein alters DNA binding. J. Biol. Chem. 274, 30849-30857.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30849-30857
    • Falcon, C.M.1    Matthews, K.S.2
  • 22
    • 0015526977 scopus 로고
    • Equilibrium and kinetic studies of Escherichia coli lac repressor-inducer interactions
    • Laiken, S. L., Gross, C. A., and von Hippel, P. H. (1972) Equilibrium and kinetic studies of Escherichia coli lac repressor-inducer interactions. J. Mol. Biol. 66, 143-155.
    • (1972) J. Mol. Biol. , vol.66 , pp. 143-155
    • Laiken, S.L.1    Gross, C.A.2    Von Hippel, P.H.3
  • 23
    • 0344412958 scopus 로고    scopus 로고
    • Perturbation from a Distance: Mutations that Alter LacI Function through Long-Range Effects
    • DOI 10.1021/bi035116x
    • Swint-Kruse, L., Zhan, H., Fairbanks, B. M., Maheshwari, A., and Matthews, K. S. (2003) Perturbation from a distance: Mutations that alter LacI function through long-range effects. Biochemistry 42, 14004-14016. (Pubitemid 37466626)
    • (2003) Biochemistry , vol.42 , Issue.47 , pp. 14004-14016
    • Swint-Kruse, L.1    Zhan, H.2    Fairbanks, B.M.3    Maheshwari, A.4    Matthews, K.S.5
  • 24
    • 0017330460 scopus 로고
    • Interaction of lac repressor with inducer. Kinetic and equilibrium measurements
    • Friedman, B. E., Olson, J. S., and Matthews, K. S. (1977) Interaction of lac repressor with inducer. Kinetic and equilibrium measurements. J. Mol. Biol. 111, 27-39.
    • (1977) J. Mol. Biol. , vol.111 , pp. 27-39
    • Friedman, B.E.1    Olson, J.S.2    Matthews, K.S.3
  • 25
    • 0022534281 scopus 로고
    • Dissociation of the lactose repressor-operator DNA complex: Effects of size and sequence context of operator-containing DNA
    • Whitson, P. A., and Matthews, K. S. (1986) Dissociation of the lactose repressor-operator DNA complex: Effects of size and sequence context of operator-containing DNA. Biochemistry 25, 3845-3852. (Pubitemid 16042511)
    • (1986) Biochemistry , vol.25 , Issue.13 , pp. 3845-3852
    • Whitson, P.A.1    Matthews, K.S.2
  • 26
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 28
    • 0032167422 scopus 로고    scopus 로고
    • Conformational changes necessary for gene regulation by Tet repressor assayed by reversible disulfide bond formation
    • DOI 10.1093/emboj/17.17.5112
    • Tiebel, B., Aung-Hilbrich, L. M., Schnappinger, D., and Hillen, W. (1998) Conformational changes necessary for gene regulation by Tet repressor assayed by reversible disulfide bond formation. EMBO J. 17, 5112-5119. (Pubitemid 28408477)
    • (1998) EMBO Journal , vol.17 , Issue.17 , pp. 5112-5119
    • Tiebel, B.1    Aung-Hilbrich, L.M.2    Schnappinger, D.3    Hillen, W.4
  • 29
    • 0023658610 scopus 로고
    • Thermodynamic analysis of inducer binding to the lactose repressor protein: Contributions of galactosyl hydroxyl groups and β substituents
    • Chakerian, A. E., Olson, J. S., and Matthews, K. S. (1987) Thermodynamic analysis of inducer binding to the lactose repressor protein: Contributions of galactosyl hydroxyl groups and β substituents. Biochemistry 26, 7250-7255.
    • (1987) Biochemistry , vol.26 , pp. 7250-7255
    • Chakerian, A.E.1    Olson, J.S.2    Matthews, K.S.3
  • 30
    • 0032502685 scopus 로고    scopus 로고
    • Kinetic and thermodynamic studies of purine repressor binding to corepressor and operator DNA
    • Xu, H., Moraitis, M., Reedstrom, R. J., and Matthews, K. S. (1998) Kinetic and thermodynamic studies of purine repressor binding to corepressor and operator DNA. J. Biol. Chem. 273, 8958-8964.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8958-8964
    • Xu, H.1    Moraitis, M.2    Reedstrom, R.J.3    Matthews, K.S.4
  • 31
    • 0017169756 scopus 로고
    • Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol
    • Yang, D. S., and Matthews, K. S. (1976) Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol. J. Mol. Biol. 103, 433-437.
    • (1976) J. Mol. Biol. , vol.103 , pp. 433-437
    • Yang, D.S.1    Matthews, K.S.2
  • 32
    • 4744347909 scopus 로고    scopus 로고
    • Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c
    • DOI 10.1021/bi0494424
    • Clarkson, M. W., and Lee, A. L. (2004) Long-range dynamic effects of point mutations propagate through side chains in the serine protease inhibitor eglin c. Biochemistry 43, 12448-12458. (Pubitemid 39314706)
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12448-12458
    • Clarkson, M.W.1    Lee, A.L.2
  • 33
    • 0035859857 scopus 로고    scopus 로고
    • Propagating conformational changes over long (and short) distances in proteins
    • Yu, E. W., and Koshland, D. E. Jr. (2001) Propagating conformational changes over long (and short) distances in proteins. Proc. Natl. Acad. Sci. U.S.A. 98, 9517-9520.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9517-9520
    • Yu, E.W.1    Koshland Jr., D.E.2
  • 34
    • 53149130515 scopus 로고    scopus 로고
    • The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity
    • Shaw, D., Wang, S. M., Villaseñor, A. G., Tsing, S., Walter, D., Browner, M. F., Barnett, J., and Kuglstatter, A. (2008) The crystal structure of JNK2 reveals conformational flexibility in the MAP kinase insert and indicates its involvement in the regulation of catalytic activity. J. Mol. Biol. 383, 885-893.
    • (2008) J. Mol. Biol. , vol.383 , pp. 885-893
    • Shaw, D.1    Wang, S.M.2    Villaseñor, A.G.3    Tsing, S.4    Walter, D.5    Browner, M.F.6    Barnett, J.7    Kuglstatter, A.8
  • 35
    • 30744478915 scopus 로고    scopus 로고
    • Protein flexibility: Its role in structure and mechanism revealed by molecular simulations
    • Dodson, G., and Verma, C. S. (2006) Protein flexibility: Its role in structure and mechanism revealed by molecular simulations. Cell. Mol. Life Sci. 63, 207-219.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 207-219
    • Dodson, G.1    Verma, C.S.2
  • 36
    • 56749176808 scopus 로고    scopus 로고
    • Dynameomics: Large-scale assessment of native protein flexibility
    • Benson, N. C., and Daggett, V. (2008) Dynameomics: Large-scale assessment of native protein flexibility. Protein Sci. 17, 2038-2050.
    • (2008) Protein Sci. , vol.17 , pp. 2038-2050
    • Benson, N.C.1    Daggett, V.2
  • 37
    • 33947419241 scopus 로고    scopus 로고
    • Local motions in a benchmark of allosteric proteins
    • DOI 10.1002/prot.21300
    • Daily, M. D., and Gray, J. J. (2007) Local motions in a benchmark of allosteric proteins. Proteins 67, 385-399. (Pubitemid 46449415)
    • (2007) Proteins: Structure, Function and Genetics , vol.67 , Issue.2 , pp. 385-399
    • Daily, M.D.1    Gray, J.J.2
  • 38
    • 61449101487 scopus 로고    scopus 로고
    • Allosteric communication occurs via networks of tertiary and quaternary motions in proteins
    • Daily, M. D., and Gray, J. J. (2009) Allosteric communication occurs via networks of tertiary and quaternary motions in proteins. PLoS Comput. Biol. 5, e1000293.
    • (2009) PLoS Comput. Biol. , vol.5
    • Daily, M.D.1    Gray, J.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.