The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
Open accessAbstract
DnaK is the canonical Hsp70 molecular chaperone protein from Escherichia coli . Like other Hsp70s, DnaK comprises two main domains: a 44-kDa N-terminal nucleotide-binding domain (NBD) that contains ATPase activity, and a 25-kDa substrate-binding domain (SBD) that harbors the substrate-binding site. Here, we report an experimental structure for wild-type, full-length DnaK, complexed with the peptide NRLLLTG and with ADP. It was obtained in aqueous solution by using NMR residual dipolar coupling and spin labeling methods and is based on available crystal structures for the isolated NBD and SBD. By using dynamics methods, we determine that the NBD and SBD are loosely linked and can move in cones of ±35° with respect to each other. The linker region between the domains is a dynamic random coil. Nevertheless, an average structure can be defined. This structure places the SBD in close proximity of subdomain IA of the NBD and suggests that the SBD collides with the NBD at this area to establish allosteric communication.
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NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,965
The Hsp70 and Hsp60 Chaperone Machines
Bukau, B., & Horwich, A. L. (1998) · Cell · doi:10.1016/s0092-8674(00)80928-9 · Cited by 2,815
Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., & Hendrickson, W. A. (1996) · Science · doi:10.1126/science.272.5268.1606 · Cited by 1,258
Nuclear Spin Relaxation in Ellipsoids Undergoing Rotational Brownian Motion
Woessner, D. E. (1962) · The Journal of Chemical Physics · doi:10.1063/1.1701390 · Cited by 904
Battiste, J. L., & Wagner, G. (2000) · Biochemistry · doi:10.1021/bi000060h · Cited by 625
Harrison, C. J., Hayer-Hartl, M., Liberto, M. D., Hartl, F.-U., & Kuriyan, J. (1997) · Science · doi:10.1126/science.276.5311.431 · Cited by 497
The Role of ATP in the Functional Cycle of the DnaK Chaperone System
McCarty, J. S., Buchberger, A., Reinstein, J., & Bukau, B. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0284 · Cited by 382
Regulation of the Escherichia coli heat‐shock response
Bukau, B. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01727.x · Cited by 341
A novel reversible thiol-specific spin label: Papain active site labeling and inhibition
Berliner, L. J., Grunwald, J., Hankovszky, H. O., & Hideg, K. (1982) · Analytical Biochemistry · doi:10.1016/0003-2697(82)90612-1 · Cited by 315
Swain, J. F., Dinler, G., Sivendran, R., Montgomery, D. L., Stotz, M., & Gierasch, L. M. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.020 · Cited by 309
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Kampinga, H. H., & Craig, E. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2941 · Cited by 1,755
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Genest, O., Wickner, S., & Doyle, S. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002806 · Cited by 382
Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones
Mayer, M. P., & Gierasch, L. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002810 · Cited by 295
Zhuravleva, A., Clerico, E. M., & Gierasch, L. M. (2012) · Cell · doi:10.1016/j.cell.2012.11.002 · Cited by 253
Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism
Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2022) · Nature · doi:10.1038/s41586-021-04252-1 · Cited by 220
Metadata
- Authors
- Bertelsen, E. B., Chang, L., Gestwicki, J. E., & Zuiderweg, E. R. P.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-05-26
- Volume
- 106
- Issue
- 21
- Pages
- 8471-8476
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2042838776
- Cited by
- 454
- References
- 36
- FWCI
- 9.96
- Type
- journal article
- Language
- en
- Open access
- green
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- Bertelsen, E. B., Chang, L., Gestwicki, J. E., & Zuiderweg, E. R. P. (2009). Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0903503106
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