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Volumn 276, Issue 5311, 1997, Pages 431-435

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN 70; NUCLEOTIDE BINDING PROTEIN; NUCLEOTIDE EXCHANGE FACTOR; PROTEIN DNAK; UNCLASSIFIED DRUG;

EID: 0030936995     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.276.5311.431     Document Type: Article
Times cited : (423)

References (38)
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    • note
    • 2-terminus [GrpE(34-197)], was as active as full-length GrpE.
  • 14
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    • note
    • Purified ATPase domain of DnaK and truncated GrpE were mixed such that there was a twofold excess of DnaK relative to the GrpE dimer. About 40 mg of complex was purified away from the excess DnaK on a Sephacryl S-100 column (2.5 cm by 63 cm) in 25 mM Mopso (pH 6.8), 25 mM NaCl, 5 mM dithiothreitol, and 10 mM (D,L)-methionine. The complex was concentrated to 200 mg/ml. Seleno-methionine-substituted DnaK and GrpE complexes, as well as complexes made with the DnaK cysteine mutants R235C and D289C (R, Arg; C, Cys; D, Asp), were prepared in the same way.
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    • 2+-NTA matrix at a slow drift rate, which was taken into account in the calculation of apparent association and dissociation rates. More than 50% of the immobilized GrpE was competent in binding DnaK.
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    • note
    • We thank A. Szabo for the initial clone of the ATPase domain of DnaK, S. Jacques for technical assistance, F. Sicheri and D. Jeruzalmi for help with data collection, A. Bohm for critically reading the manuscript, and H. Nelson, T. Alber, and his group for helpful discussions. The 2.8 Å data set was measured at the Cornell High Energy Synchrotron Source. The coordinates have been deposited in the Brookhaven Protein Data Bank with the accession code 1DKG.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.