1q5l
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NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG
Overview
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.
About this Structure
1Q5L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG., Stevens SY, Cai S, Pellecchia M, Zuiderweg ER, Protein Sci. 2003 Nov;12(11):2588-96. PMID:14573869
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