1Q5L

NMR structure of the substrate binding domain of DnaK bound to the peptide NRLLLTG

Summary for 1Q5L

• Entry DOI: 10.2210/pdb1q5l/pdb
• Related: 1BPR 1DG4 1DKX
• Descriptor: Chaperone protein dnaK, peptide NRLLLTG (2 entities in total)
• Functional Keywords: hsp70, chaperone, heat shock protein
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A6Y8
• Total number of polymer chains: 2
• Total formula weight: 15258.29

Authors

Stevens, S.Y.,Cai, S.,Pellecchia, M.,Zuiderweg, E.R. (deposition date: 2003-08-08, release date: 2003-11-04, Last modification date: 2024-05-22)

Primary citation

Stevens, S.Y.,Cai, S.,Pellecchia, M.,Zuiderweg, E.R.
The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG.
Protein Sci., 12:2588-2596, 2003

PubMed 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.

PubMed: 14573869
DOI: 10.1110/ps.03269103

Experimental method

SOLUTION NMR