PMID:14573869
| Citation |
Stevens, SY, Cai, S, Pellecchia, M and Zuiderweg, ER (2003) The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG. Protein Sci. 12:2588-96 |
|---|---|
| Abstract |
The Hsp70 family of molecular chaperones participates in a number of cellular processes, including binding to nascent polypeptide chains and assistance in protein (re)folding and degradation. We present the solution structure of the substrate binding domain (residues 393-507) of the Escherichia coli Hsp70, DnaK, that is bound to the peptide NRLLLTG and compare it to the crystal structure of DnaK(389-607) bound to the same peptide. The construct discussed here does not contain the alpha-helical domain that characterizes earlier published peptide-bound structures of the Hsp70s. It is established that removing the alpha-helical domain in its entirety does not affect the primary interactions or structure of the DnaK(393-507) in complex with the peptide NRLLLTG. In particular, the arch that protects the substrate-binding cleft is also formed in the absence of the helical lid. 15N-relaxation measurements show that the peptide-bound form of DnaK(393-507) is relatively rigid. As compared to the peptide-free state, the peptide-bound state of the domain shows distinct, widespread, and contiguous differences in structure extending toward areas previously defined as important to the allosteric regulation of the Hsp70 chaperones. |
| Links |
PubMed PMC2366956 Online version:10.1110/ps.03269103 |
| Keywords |
Allosteric Regulation; Amino Acid Sequence; Crystallography, X-Ray; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/metabolism; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Oligopeptides/chemistry; Oligopeptides/metabolism; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Solutions |
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