Peptide-Induced Conformational Changes in the Molecular Chaperone DnaK

DnaK, the 70 kDa molecular chaperone of Escherichia coli, adopts a high-affinity state in the presence of ADP that tightly binds its target peptide, whereas replacement of ADP by ATP induces a structural switch to a low-affinity chaperone state that weakly binds its target. An ∼15% decrease in trypt...

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Veröffentlicht in:	Biochemistry (Easton) 1998-11, Vol.37 (47), p.16749-16756
Hauptverfasser:	Slepenkov, Sergey V, Witt, Stephan N
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism DNA-Binding Proteins Escherichia coli Escherichia coli Proteins HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - metabolism Kinetics Macromolecular Substances Models, Chemical Peptides - pharmacology Protein Binding Protein Conformation - drug effects Repressor Proteins - chemistry Repressor Proteins - metabolism Spectrometry, Fluorescence Tryptophan - metabolism Viral Proteins Viral Regulatory and Accessory Proteins
Online-Zugang:	Volltext
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