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Molecular chaperones in cellular protein folding
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Hartl F.U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
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Hartl, F.U.1
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0031684079
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Structure and function in GroEL-mediated protein folding
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Sigler P.B., Xu Z., Rye H.S., Burston S.G., Fenton W.A., Horwich A.L. Structure and function in GroEL-mediated protein folding. Annu Rev Biochem. 67:1998;581-607.
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The Hsp70 and Hsp60 chaperone machines
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Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366.
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Structural aspects of GroEL function
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Horovitz A. Structural aspects of GroEL function. Curr Opin Struct Biol. 8:1998;93-100.
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Principles of protein folding in the cellular environment
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Curr Opin Struct Biol
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Ellis, R.J.1
Hartl, F.U.2
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9
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0027943510
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The crystal structure of the bacterial chaperonin GroEL at 2.8 Å resolution
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Braig K., Otwinowski Z., Hegde R., Boisvert D.C., Joachimiak A., Horwich A.L., Sigler P.B. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å resolution. Nature. 371:1994;578-586.
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Nature
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Braig, K.1
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Joachimiak, A.5
Horwich, A.L.6
Sigler, P.B.7
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10
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0028027055
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Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
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Chen S., Roseman A.M., Hunter A.S., Wood S.P., Burston S.G., Ranson N.A., Clarke A.R., Saibil H.R. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature. 371:1994;261-264.
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Nature
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Chen, S.1
Roseman, A.M.2
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Wood, S.P.4
Burston, S.G.5
Ranson, N.A.6
Clarke, A.R.7
Saibil, H.R.8
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11
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0030592538
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The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
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Roseman A.M., Chen S., White H., Braig K., Saibil H.R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
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Roseman, A.M.1
Chen, S.2
White, H.3
Braig, K.4
Saibil, H.R.5
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13
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0029004759
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Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
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Yifrach O., Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry. 34:1995;5303-5308.
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Yifrach, O.1
Horovitz, A.2
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14
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0032546571
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Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL
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A tryptophan reporter was used to demonstrate that protein conformational changes follow the nested positive/negative cooperativity scheme proposed earlier on the basis of steady-state studies of ATP binding [13].
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Yifrach O., Horovitz A. Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL. Biochemistry. 37:1998;7083-7088. A tryptophan reporter was used to demonstrate that protein conformational changes follow the nested positive/negative cooperativity scheme proposed earlier on the basis of steady-state studies of ATP binding [13].
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Biochemistry
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Yifrach, O.1
Horovitz, A.2
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15
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0032714370
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A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL
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The use of a different tryptophan reporter and faster kinetics measurements demonstrates a series of conformational changes and suggests the presence of intermediate states during ATP and GroES binding, and substrate release.
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Cliff M.J., Kad N.M., Hay N., Lund P.A., Webb M.R., Burston S.G., Clarke A.R. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL. J Mol Biol. 293:1999;667-684. The use of a different tryptophan reporter and faster kinetics measurements demonstrates a series of conformational changes and suggests the presence of intermediate states during ATP and GroES binding, and substrate release.
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(1999)
J Mol Biol
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Cliff, M.J.1
Kad, N.M.2
Hay, N.3
Lund, P.A.4
Webb, M.R.5
Burston, S.G.6
Clarke, A.R.7
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16
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0034652350
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Coupling between protein folding and allostery in the GroE chaperonin system
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The effects of positive and negative cooperativity on the GroEL-assisted folding rates of two proteins were measured using a set of previously characterised GroEL mutants with altered cooperativities. Strong intra-ring positive cooperativity slows the folding of a fast folder that is not dependent on GroES, by slowing the allosteric transition leading to substrate release. Strong negative cooperativity also slows its folding in the absence of GroES, but accelerates it in the presence of GroES. These results are attributed to effects on the kinetic partitioning between folding in solution or inside the complex. For a slower folding substrate that is dependent on GroES, folding rates are largely independent of cooperativity, as folding only takes place inside the complex. The work demonstrates the balance achieved by the GroE mechanism to allow the efficient folding of diverse substrates.
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Yifrach O., Horovitz A. Coupling between protein folding and allostery in the GroE chaperonin system. Proc Natl Acad Sci USA. 97:2000;1521-1524. The effects of positive and negative cooperativity on the GroEL-assisted folding rates of two proteins were measured using a set of previously characterised GroEL mutants with altered cooperativities. Strong intra-ring positive cooperativity slows the folding of a fast folder that is not dependent on GroES, by slowing the allosteric transition leading to substrate release. Strong negative cooperativity also slows its folding in the absence of GroES, but accelerates it in the presence of GroES. These results are attributed to effects on the kinetic partitioning between folding in solution or inside the complex. For a slower folding substrate that is dependent on GroES, folding rates are largely independent of cooperativity, as folding only takes place inside the complex. The work demonstrates the balance achieved by the GroE mechanism to allow the efficient folding of diverse substrates.
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(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 1521-1524
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Yifrach, O.1
Horovitz, A.2
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17
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0032555216
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The allosteric mechanism of the chaperonin GroEL: A dynamic analysis
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A novel molecular dynamics approach was used to investigate vibrational modes of the GroEL subunit and inter-ring interface. Hinge rotations and domain twisting are shown to arise from the intrinsic flexibility of the subunits. The results are compatible with structural studies and reinforce the idea that the allosteric movements occur about hinges within the subunits, rather than being relative motions between subunits, as previously described for classical allosteric systems.
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Ma J., Karplus M. The allosteric mechanism of the chaperonin GroEL: a dynamic analysis. Proc Natl Acad Sci USA. 95:1998;8502-8507. A novel molecular dynamics approach was used to investigate vibrational modes of the GroEL subunit and inter-ring interface. Hinge rotations and domain twisting are shown to arise from the intrinsic flexibility of the subunits. The results are compatible with structural studies and reinforce the idea that the allosteric movements occur about hinges within the subunits, rather than being relative motions between subunits, as previously described for classical allosteric systems.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 8502-8507
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Ma, J.1
Karplus, M.2
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0028031345
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Dynamics of the chaperonin ATPase cycle: Implications for the mechanism of assisted protein folding
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Todd M.J., Viitanen P.V., Lorimer G.H. Dynamics of the chaperonin ATPase cycle: implications for the mechanism of assisted protein folding. Science. 265:1994;659-666.
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Science
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Todd, M.J.1
Viitanen, P.V.2
Lorimer, G.H.3
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19
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0027933369
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GroEL-mediated protein folding proceeds by multiple rounds of binding and release of non-native forms
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Weissman J.S., Kashi Y., Fenton W.A., Horwich A.L. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of non-native forms. Cell. 78:1994;693-702.
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Weissman, J.S.1
Kashi, Y.2
Fenton, W.A.3
Horwich, A.L.4
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20
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0030804446
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Distinct actions of cis and trans ATP binding within the double ring of the chaperonin GroEL
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Rye H.S., Burston S.G., Beechem J.M., Xu Z., Sigler P.B., Horwich A.L. Distinct actions of cis and trans ATP binding within the double ring of the chaperonin GroEL. Nature. 388:1997;792-798.
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Rye, H.S.1
Burston, S.G.2
Beechem, J.M.3
Xu, Z.4
Sigler, P.B.5
Horwich, A.L.6
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21
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0032562652
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Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings
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Kad N.M., Ranson N.A., Cliff M.J., Clarke A.R. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings. J Mol Biol. 278:1998;267-278.
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J Mol Biol
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Kad, N.M.1
Ranson, N.A.2
Cliff, M.J.3
Clarke, A.R.4
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22
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0033617129
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GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings
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This very detailed fluorescence energy transfer study, coupled with cryo-electron microscopy, shows an ordered sequence of substrate interactions with the alternating acceptor and folding rings of the GroE complexes.
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Rye H.S., Roseman A.M., Chen S., Furtak K., Fenton W.A., Saibil H.R., Horwich A.L. GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings. Cell. 97:1999;325-338. This very detailed fluorescence energy transfer study, coupled with cryo-electron microscopy, shows an ordered sequence of substrate interactions with the alternating acceptor and folding rings of the GroE complexes.
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(1999)
Cell
, vol.97
, pp. 325-338
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Rye, H.S.1
Roseman, A.M.2
Chen, S.3
Furtak, K.4
Fenton, W.A.5
Saibil, H.R.6
Horwich, A.L.7
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23
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0033543656
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GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices
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A set of peptides that bind to the isolated apical domain of GroEL was generated by random mutagenesis of the binding surface of the fungal enzyme cellobiohydrolase I. Seven discontinuous residues bind in a similar manner as the GroES mobile loop and as the previously studied binding peptide from an N-terminal tag. The positions of binding residues are compatible with extended, α or β conformations.
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Chatellier J., Buckle A.M., Fersht A.R. GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices. J Mol Biol. 292:1999;163-172. A set of peptides that bind to the isolated apical domain of GroEL was generated by random mutagenesis of the binding surface of the fungal enzyme cellobiohydrolase I. Seven discontinuous residues bind in a similar manner as the GroES mobile loop and as the previously studied binding peptide from an N-terminal tag. The positions of binding residues are compatible with extended, α or β conformations.
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(1999)
J Mol Biol
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Chatellier, J.1
Buckle, A.M.2
Fersht, A.R.3
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24
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0033598941
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The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
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Phage display was used to generate peptides that bind strongly to the isolated apical domain of GroEL from random 12-mers. The crystal structure of the tightest complex was determined and the complex of 14 copies of the peptide bound to intact GroEL was crystallised and partially refined. Adjustments of the apical domain conformation to the bound peptide were observed when comparing the different peptide complexes.
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Chen L., Sigler P.B. The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity. Cell. 99:1999;757-768. Phage display was used to generate peptides that bind strongly to the isolated apical domain of GroEL from random 12-mers. The crystal structure of the tightest complex was determined and the complex of 14 copies of the peptide bound to intact GroEL was crystallised and partially refined. Adjustments of the apical domain conformation to the bound peptide were observed when comparing the different peptide complexes.
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(1999)
Cell
, vol.99
, pp. 757-768
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Chen, L.1
Sigler, P.B.2
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26
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0033543736
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NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution
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Kobayashi N., Freund S.M.V., Chatellier J., Zahn R., Fersht A.R. NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution. J Mol Biol. 292:1999;181-190.
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(1999)
J Mol Biol
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Kobayashi, N.1
Freund, S.M.V.2
Chatellier, J.3
Zahn, R.4
Fersht, A.R.5
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27
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0028113299
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Residues in the chaperonin GroEL required for polypeptide binding and release
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Fenton W.A., Kashi Y., Furtak K., Horwich A.L. Residues in the chaperonin GroEL required for polypeptide binding and release. Nature. 371:1994;614-619.
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Nature
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Fenton, W.A.1
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Horwich, A.L.4
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28
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0033547324
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Identification of in vivo substrates of the chaperonin GroEL
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Houry W.A., Frishman D., Eckerskorn C., Lottspeich F., Hartl F.U. Identification of in vivo substrates of the chaperonin GroEL. Nature. 402:1999;147-154.
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Nature
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Houry, W.A.1
Frishman, D.2
Eckerskorn, C.3
Lottspeich, F.4
Hartl, F.U.5
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29
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0027419011
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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle - Implications for the mechanism of assisted protein folding
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Jackson G.S., Staniforth R.A., Halsall D.J., Atkinson T., Holbrook J.J., Clarke A.R., Burston S.G. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle - implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;2554-2563.
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Biochemistry
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Jackson, G.S.1
Staniforth, R.A.2
Halsall, D.J.3
Atkinson, T.4
Holbrook, J.J.5
Clarke, A.R.6
Burston, S.G.7
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30
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0030576536
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Conformational states bound by the molecular chaperones GroEL and SecB: A hidden unfolding (annealing) activity
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Zahn R., Perrett S., Fersht A.R. Conformational states bound by the molecular chaperones GroEL and SecB: a hidden unfolding (annealing) activity. J Mol Biol. 261:1996;43-61.
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J Mol Biol
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Zahn, R.1
Perrett, S.2
Fersht, A.R.3
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31
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0033617534
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Chaperonin function: Folding by forced unfolding
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Hydrogen exchange was monitored in a protein interacting with the GroEL-GroES-ATP system, showing that the interaction causes substantial unfolding. The results are used to support the idea of mechanical unfolding caused by the spatial separation of GroEL binding sites during the hinge rotations leading to GroES binding.
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Shtilerman M., Lorimer G.H., Englander S.W. Chaperonin function: folding by forced unfolding. Science. 284:1999;822-825. Hydrogen exchange was monitored in a protein interacting with the GroEL-GroES-ATP system, showing that the interaction causes substantial unfolding. The results are used to support the idea of mechanical unfolding caused by the spatial separation of GroEL binding sites during the hinge rotations leading to GroES binding.
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(1999)
Science
, vol.284
, pp. 822-825
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Shtilerman, M.1
Lorimer, G.H.2
Englander, S.W.3
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32
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0034598920
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Multivalent binding of non-native substrate proteins by the chaperonin GroEL
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All seven subunits of a GroEL ring were expressed as one chain and shown to dimerise into a relatively functional assembly. Full function is obtained if the connected N and C termini are proteolytically cleaved. In combination with mutations that inactivate substrate binding by apical domains, this construct was used to test the number and arrangement of functional domains necessary for GroE function. Three adjacent functional domains appear to be the minimum required.
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Farr G.W., Furtak K., Rowland M.B., Ranson N.A., Saibil H.R., Kirchhausen T., Horwich A.L. Multivalent binding of non-native substrate proteins by the chaperonin GroEL. Cell. 100:2000;561-573. All seven subunits of a GroEL ring were expressed as one chain and shown to dimerise into a relatively functional assembly. Full function is obtained if the connected N and C termini are proteolytically cleaved. In combination with mutations that inactivate substrate binding by apical domains, this construct was used to test the number and arrangement of functional domains necessary for GroE function. Three adjacent functional domains appear to be the minimum required.
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(2000)
Cell
, vol.100
, pp. 561-573
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Farr, G.W.1
Furtak, K.2
Rowland, M.B.3
Ranson, N.A.4
Saibil, H.R.5
Kirchhausen, T.6
Horwich, A.L.7
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33
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0032478545
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Crystal structure of the thermosome, the archaeal chaperonin and homolog to CCT
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The structure of the thermosome 16-mer reveals how the long protrusion on the apical domains joins up to form a built-in lid, replacing the function of GroES. Another surprise is the interface between the two rings, which has a different arrangement from that in GroEL. Despite the presence or absence of various nucleotides, only a fully closed form is observed in the crystals.
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Ditzel L., Löwe J., Stock D., Stetter K.O., Huber H., Huber R., Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog to CCT. Cell. 93:1998;125-138. The structure of the thermosome 16-mer reveals how the long protrusion on the apical domains joins up to form a built-in lid, replacing the function of GroES. Another surprise is the interface between the two rings, which has a different arrangement from that in GroEL. Despite the presence or absence of various nucleotides, only a fully closed form is observed in the crystals.
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(1998)
Cell
, vol.93
, pp. 125-138
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Ditzel, L.1
Löwe, J.2
Stock, D.3
Stetter, K.O.4
Huber, H.5
Huber, R.6
Steinbacher, S.7
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34
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0032701797
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Group II chaperonins: New TRiC(k)s and turns of a protein folding machine
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Gutsche I., Essen L.O., Baumeister W. Group II chaperonins: new TRiC(k)s and turns of a protein folding machine. J Mol Biol. 293:1999;295-312.
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(1999)
J Mol Biol
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Gutsche, I.1
Essen, L.O.2
Baumeister, W.3
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35
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0030668929
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Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
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Klumpp M., Baumeister W., Essen L.O. Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell. 91:1997;263-270.
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(1997)
Cell
, vol.91
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Klumpp, M.1
Baumeister, W.2
Essen, L.O.3
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36
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0031719642
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Group II chaperonin in an open conformation examined by electron tomography
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Nitsch M., Walz J., Typke D., Klumpp M., Essen L-O., Baumeister W. Group II chaperonin in an open conformation examined by electron tomography. Nat Struct Biol. 5:1998;855-857.
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(1998)
Nat Struct Biol
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Nitsch, M.1
Walz, J.2
Typke, D.3
Klumpp, M.4
Essen, L.-O.5
Baumeister, W.6
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37
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0034711948
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Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae
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Schoehn G., Quaite-Randall E., Jimenez J.L., Joachimiak A., Saibil H.R. Three conformations of an archaeal chaperonin, TF55 from Sulfolobus shibatae. J Mol Biol. 296:2000;813-819.
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(2000)
J Mol Biol
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Schoehn, G.1
Quaite-Randall, E.2
Jimenez, J.L.3
Joachimiak, A.4
Saibil, H.R.5
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38
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0032985364
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3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin
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Llorca O., Smyth M.G., Carrascosa J.L., Willison K.R., Radermacher M., Steinbacher S., Valpuesta J.M. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin. Nat Struct Biol. 7:1999;639-642.
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(1999)
Nat Struct Biol
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Llorca, O.1
Smyth, M.G.2
Carrascosa, J.L.3
Willison, K.R.4
Radermacher, M.5
Steinbacher, S.6
Valpuesta, J.M.7
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39
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0032549677
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The small heat-shock protein, αb-crystallin, has a variable quaternary structure
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Haley D.A., Horwitz J., Stewart P.L. The small heat-shock protein, αB-crystallin, has a variable quaternary structure. J Mol Biol. 277:1998;27-35.
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(1998)
J Mol Biol
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Haley, D.A.1
Horwitz, J.2
Stewart, P.L.3
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40
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1342292267
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Crystal structure of a small heat-shock protein
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The first structure of a member of the α-crystallin family reveals an immunoglobulin fold for the conserved domain. This archaeal small heat-shock protein from Methanococcus jannaschi is a hollow shell of 24 subunits with octahedral symmetry.
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Kim K.K., Kim R., Kim S.H. Crystal structure of a small heat-shock protein. Nature. 394:1998;595-599. The first structure of a member of the α-crystallin family reveals an immunoglobulin fold for the conserved domain. This archaeal small heat-shock protein from Methanococcus jannaschi is a hollow shell of 24 subunits with octahedral symmetry.
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(1998)
Nature
, vol.394
, pp. 595-599
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Kim, K.K.1
Kim, R.2
Kim, S.H.3
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41
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0031024691
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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
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Lee G.J., Roseman A.M., Saibil H.R., Vierling E. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16:1997;659-671.
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(1997)
EMBO J
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Lee, G.J.1
Roseman, A.M.2
Saibil, H.R.3
Vierling, E.4
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42
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0033485868
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Hsp26: A temperature-regulated chaperone
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Haslbeck M., Walke S., Stromer T., Ehrnsperger M., White H.E., Chen S., Saibil H.R., Buchner J. Hsp26: a temperature-regulated chaperone. EMBO J. 18:1999;6744-6751.
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(1999)
EMBO J
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Haslbeck, M.1
Walke, S.2
Stromer, T.3
Ehrnsperger, M.4
White, H.E.5
Chen, S.6
Saibil, H.R.7
Buchner, J.8
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43
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0024468229
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Crystal structure of chaperone protein PapD reveals an immunoglobulin fold
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Holmgren A., Branden C.I. Crystal structure of chaperone protein PapD reveals an immunoglobulin fold. Nature. 342:1989;248-251.
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(1989)
Nature
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Holmgren, A.1
Branden, C.I.2
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46
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0033551911
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X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli
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••] report chaperone-substrate complexes with two different forms of bacterial pilin. Although the structures are somewhat different, they both reveal a new mechanism of chaperone action. The immunoglobulin fold of the substrate is missing an edge strand, exposing its hydrophobic core. The chaperone donates an edge strand and accompanies the pilin to the outer membrane, where it is exported to form the growing pilus. In the pilus assembly, each pilin supplies an edge strand to its neighbour.
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••] report chaperone-substrate complexes with two different forms of bacterial pilin. Although the structures are somewhat different, they both reveal a new mechanism of chaperone action. The immunoglobulin fold of the substrate is missing an edge strand, exposing its hydrophobic core. The chaperone donates an edge strand and accompanies the pilin to the outer membrane, where it is exported to form the growing pilus. In the pilus assembly, each pilin supplies an edge strand to its neighbour.
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Choudhury, D.1
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An extremely useful review that defines a large protein family with extremely diverse membership.
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Neuwald A.F., Aravind L., Spouge J.L., Koonin E.V. AAA+: a class of chaperone-like ATPases associated with the assembly, operation and disassembly of protein complexes. Genome Res. 9:1999;27-43. An extremely useful review that defines a large protein family with extremely diverse membership.
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Neuwald, A.F.1
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Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
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•] report a mechanism for rescuing protein from aggregates involving the cooperation of two ATP-dependent chaperone systems - the Hsp100/Clp family solubilises the aggregated protein and releases it in a state that can be refolded by the Hsp70 system. The first case is demonstrated in yeast and the second study is in E. coli.
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•] report a mechanism for rescuing protein from aggregates involving the cooperation of two ATP-dependent chaperone systems - the Hsp100/Clp family solubilises the aggregated protein and releases it in a state that can be refolded by the Hsp70 system. The first case is demonstrated in yeast and the second study is in E. coli.
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Proc Natl Acad Sci USA
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Goloubinoff, P.1
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Bukau, B.6
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53
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0033517351
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Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
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A remarkable demonstration of the unfolding ability of a bacterial Hsp100 controlled by a specific recognition sequence. The stable green fluorescent protein is totally unfolded by ClpA in the presence of ATP if it is tagged with the 11-residue recognition sequence at its C terminus.
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Weber-Ban E.U., Reid B.G., Miranker A.D., Horwich A.L. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature. 401:1999;90-93. A remarkable demonstration of the unfolding ability of a bacterial Hsp100 controlled by a specific recognition sequence. The stable green fluorescent protein is totally unfolded by ClpA in the presence of ATP if it is tagged with the 11-residue recognition sequence at its C terminus.
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Nature
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Weber-Ban, E.U.1
Reid, B.G.2
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54
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0032215219
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At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
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A low-resolution cryo-EM map of the ClpA-ClpP assembly shows its similarity to the proteasome and suggests that the curious symmetry mismatch may be involved with a rotatory action. The ClpA map shows the two-tiered ring structure formed by the hexamer of subunits, each containing two AAA modules.
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Beuron F., Maurizi M.R., Belnap D.M., Kocsis E., Booy F.P., Kessel M., Steven A.C. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J Struct Biol. 123:1998;248-259. A low-resolution cryo-EM map of the ClpA-ClpP assembly shows its similarity to the proteasome and suggests that the curious symmetry mismatch may be involved with a rotatory action. The ClpA map shows the two-tiered ring structure formed by the hexamer of subunits, each containing two AAA modules.
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Beuron, F.1
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Steven, A.C.7
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56
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Structure of the ATP dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
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•] report the structure of an AAA ATPase module. N-ethylmaleimide sensitive factor (NSF) has two AAA modules and the one determined in both studies is necessary for hexamer formation. The structures reveal the nucleotide-binding site and oligomer assembly. The similarity to the δ′ clamp-loader subunit of DNA polymerase III helps to define the conserved elements in the superfamily. The module consists of a wedge-shaped nucleotide-binding domain, which forms the body of the hexamer, and a projecting helical domain.
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•] report the structure of an AAA ATPase module. N-ethylmaleimide sensitive factor (NSF) has two AAA modules and the one determined in both studies is necessary for hexamer formation. The structures reveal the nucleotide-binding site and oligomer assembly. The similarity to the δ′ clamp-loader subunit of DNA polymerase III helps to define the conserved elements in the superfamily. The module consists of a wedge-shaped nucleotide-binding domain, which forms the body of the hexamer, and a projecting helical domain.
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Nat Struct Biol
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Yu, R.C.1
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57
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The structures of HslU and the ATP-dependent protease HslU-HslV
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This paper reports crystal structures of the hexameric Hsp100 HslU alone and in complex with the double-ring protease HslV, which also has sixfold symmetry. The two major domains of HslU are connected by a flexible hinge region and rotate into a more closed conformation in the presence of bound nucleotide. These two domains clearly have the same fold as the other AAA modules. In addition, a long extension of the nucleotide-binding domain contacts HslV.
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Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R. The structures of HslU and the ATP-dependent protease HslU-HslV. Nature. 403:2000;800-805. This paper reports crystal structures of the hexameric Hsp100 HslU alone and in complex with the double-ring protease HslV, which also has sixfold symmetry. The two major domains of HslU are connected by a flexible hinge region and rotate into a more closed conformation in the presence of bound nucleotide. These two domains clearly have the same fold as the other AAA modules. In addition, a long extension of the nucleotide-binding domain contacts HslV.
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(2000)
Nature
, vol.403
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Bochtler, M.1
Hartmann, C.2
Song, H.K.3
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Huber, R.6
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58
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The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome
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Rohrwild M., Pfeifer G., Santarius U., Muller S.A., Huang H.C., Engel A., Baumeister W., Goldberg A.L. The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome. Nat Struct Biol. 4:1997;133-139.
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Rohrwild, M.1
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Baumeister, W.7
Goldberg, A.L.8
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59
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Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
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60
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0033573135
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Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
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Mogk A., Tomoyasu T., Goloubinoff P., Rüdiger S., Röder D., Langen H., Bukau B. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18:1999;6934-6949.
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Mogk, A.1
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Kraulis P.J. Molscript- a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
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