PMID:10048327
| Citation |
Bertelsen, EB, Zhou, H, Lowry, DF, Flynn, GC and Dahlquist, FW (1999) Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution. Protein Sci. 8:343-54 |
|---|---|
| Abstract |
Hsp70 molecular chaperones contain three distinct structural domains, a 44 kDa N-terminal ATPase domain, a 17 kDa peptide-binding domain, and a 10 kDa C-terminal domain. The ATPase and peptide binding domains are conserved in sequence and are functionally well characterized. The function of the 10 kDa variable C-terminal domain is less well understood. We have characterized the secondary structure and dynamics of the C-terminal domain from the Escherichia coli Hsp70, DnaK, in solution by high-resolution NMR. The domain was shown to be comprised of a rigid structure consisting of four helices and a flexible C-terminal subdomain of approximately 33 amino acids. The mobility of the flexible region is maintained in the context of the full-length protein and does not appear to be modulated by the nucleotide state. The flexibility of this region appears to be a conserved feature of Hsp70 architecture and may have important functional implications. We also developed a method to analyze 15N nuclear spin relaxation data, which allows us to extract amide bond vector directions relative to a unique diffusion axis. The extracted angles and rotational correlation times indicate that the helices form an elongated, bundle-like structure in solution. |
| Links |
PubMed PMC2144266 Online version:10.1110/ps.8.2.343 |
| Keywords |
Amino Acid Sequence; Escherichia coli/chemistry; Escherichia coli Proteins; HSP70 Heat-Shock Proteins/analysis; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary |
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