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

Science

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

  Harrison, Celia J ^a,c   Hayer Hartl, Manajit ^b,c   Di Liberto, Maurizio ^b,c   Hartl, F Ulrich ^b,c   Kuriyan, John ^a,c  

^a ROCKEFELLER UNIVERSITY   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

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

ALPHA HELIX; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ESCHERICHIA COLI PROTEINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

ESCHERICHIA; ESCHERICHIA COLI; MAMMALIA;

EID: 0030936995     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.276.5311.431     Document Type: Article

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38. 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.