메뉴 건너뛰기




Volumn 11, Issue 12, 2003, Pages 1475-1483

The Crystal Structure of the Yeast Hsp40 Ydj1 Complexed with Its Peptide Substrate

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLYCYLTRYPTOPHYLLEUCYLTYROSYLGLUTAMYLISOLEUCYLSERINE; LEUCINE; PEPTIDE FRAGMENT; UNCLASSIFIED DRUG;

EID: 0345299781     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.10.012     Document Type: Article
Times cited : (146)

References (30)
  • 3
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 4
    • 0025745326 scopus 로고
    • Characterization of Ydj1: A yeast homologue of the bacteria dnaJ protein
    • Caplan A.J., Douglas M.G. Characterization of Ydj1. a yeast homologue of the bacteria dnaJ protein J. Cell Biol. 114:1991;609-621.
    • (1991) J. Cell Biol. , vol.114 , pp. 609-621
    • Caplan, A.J.1    Douglas, M.G.2
  • 5
    • 0000449348 scopus 로고
    • Ribbons 2.0. Ribbon models for macromolecule
    • Carson M. Ribbons 2.0. Ribbon models for macromolecule. J. Mol. Graph. 5:1987;103-106.
    • (1987) J. Mol. Graph. , vol.5 , pp. 103-106
    • Carson, M.1
  • 6
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide comlex: Plasticity as a basis for substrate diversity
    • Chen L., Sigler P.B. The crystal structure of a GroEL/peptide comlex. plasticity as a basis for substrate diversity Cell. 99:1999;757-768.
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 7
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone Bip
    • Flynn G.C., Pohl J., Flocco M.T., Rothman J.E. Peptide-binding specificity of the molecular chaperone Bip. Nature. 353:1991;726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 8
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 9
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl F.U., Hayer-Hartl M. Molecular chaperones in the cytosol. from nascent chain to folded protein Science. 295:2002;1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 10
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science. 254:1991;51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 11
    • 0035911158 scopus 로고    scopus 로고
    • An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae
    • Johnson J.L., Craig E.A. An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J. Cell Biol. 152:2001;851-856.
    • (2001) J. Cell Biol. , vol.152 , pp. 851-856
    • Johnson, J.L.1    Craig, E.A.2
  • 12
    • 84889120137 scopus 로고
    • Improved methods for building protein models in the electron density maps and the location of errors in these maps
    • Jones T.A., Zhou J.Y., Cowan S.W., Kjeldgard M. Improved methods for building protein models in the electron density maps and the location of errors in these maps. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgard, M.4
  • 13
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T., Lu C., Echols H., Flanagan J., Hayer M.K., Hartl F.U. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature. 356:1992;683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 15
    • 0037077211 scopus 로고    scopus 로고
    • Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding
    • Lee S., Fan C.Y., Younger J.M., Ren H., Cyr D.M. Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding. J. Biol. Chem. 277:2002;21675-21682.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21675-21682
    • Lee, S.1    Fan, C.Y.2    Younger, J.M.3    Ren, H.4    Cyr, D.M.5
  • 16
    • 0032561360 scopus 로고    scopus 로고
    • Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperone Sis1 and Ydj1
    • Lu Z., Cyr D.M. Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperone Sis1 and Ydj1. J. Biol. Chem. 273:1998;27824-27830.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27824-27830
    • Lu, Z.1    Cyr, D.M.2
  • 17
    • 0034698002 scopus 로고    scopus 로고
    • Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ
    • Martinez-Yamout M., Legge G.B., Zhang O., Wright P.E., Dyson H.J. Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. J. Mol. Biol. 300:2000;805-818.
    • (2000) J. Mol. Biol. , vol.300 , pp. 805-818
    • Martinez-Yamout, M.1    Legge, G.B.2    Zhang, O.3    Wright, P.E.4    Dyson, H.J.5
  • 18
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33:1968;491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 19
    • 0032214832 scopus 로고    scopus 로고
    • J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
    • Misselwitz S., Staeck O., Rapoport T.A. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol. Cell. 2:1998;593-603.
    • (1998) Mol. Cell , vol.2 , pp. 593-603
    • Misselwitz, S.1    Staeck, O.2    Rapoport, T.A.3
  • 20
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins. 11:1991;281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 0036177548 scopus 로고    scopus 로고
    • Direct interactions between molecular chaperones Hsp70 and Hsp40: Yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1
    • Qian X., Hou W., Li Z., Sha B.D. Direct interactions between molecular chaperones Hsp70 and Hsp40. yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1 Biochem. J. 361:2002;27-34.
    • (2002) Biochem. J. , vol.361 , pp. 27-34
    • Qian, X.1    Hou, W.2    Li, Z.3    Sha, B.D.4
  • 23
    • 0035283043 scopus 로고    scopus 로고
    • Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
    • Rudiger S., Schneider-Mergener J., Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J. 20:2001;1042-1050.
    • (2001) EMBO J. , vol.20 , pp. 1042-1050
    • Rudiger, S.1    Schneider-Mergener, J.2    Bukau, B.3
  • 24
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • Sauer F.G., Pinkner J.S., Waksman G., Hultgren S.J. Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell. 111:2002;543-551.
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 25
  • 26
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott J.K., Smith G.P. Searching for peptide ligands with an epitope library. Science. 249:1990;386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 27
    • 0034662746 scopus 로고    scopus 로고
    • The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
    • Sha B.D., Lee S., Cyr D.M. The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure. 8:2000;799-807.
    • (2000) Structure , vol.8 , pp. 799-807
    • Sha, B.D.1    Lee, S.2    Cyr, D.M.3
  • 28
    • 0030030946 scopus 로고    scopus 로고
    • A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
    • Szabo A., Korszun R., Hartl F.U., Flanagan J. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J. 15:1996;408-417.
    • (1996) EMBO J. , vol.15 , pp. 408-417
    • Szabo, A.1    Korszun, R.2    Hartl, F.U.3    Flanagan, J.4
  • 29
    • 0028170215 scopus 로고
    • The N-terminal 108 amino acid of the E. coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lamda replication
    • Wall D., Zylicz M., Georgopoulos C. The N-terminal 108 amino acid of the E. coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lamda replication. J. Biol. Chem. 269:1994;5446-5451.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.