Journal article
Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution
Protein science, Vol.8(2), pp.343-354
02/1999
Handle:
https://hdl.handle.net/2376/108127
PMID: 10048327
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.
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Details
- Title
- Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution
- Creators
- ERIC B BERTELSEN - Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403HONGJUN ZHOU - Macromolecular NMR Section, ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, Frederick, Maryland 21702DAVID F LOWRY - Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, 902 Battelle Boulevard, Richland, Washington 99352GREGORY C FLYNN - Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403FREDERICK W DAHLQUIST - Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403
- Publication Details
- Protein science, Vol.8(2), pp.343-354
- Academic Unit
- Engineering and Applied Sciences (TRIC), School of
- Publisher
- Cambridge University Press
- Number of pages
- 12
- Identifiers
- 99900547759101842
- Language
- English
- Resource Type
- Journal article