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Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
Open accessAbstract
DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 Å resolution. The structure consists of a β-sandwich subdomain followed by α-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the β sandwich. An α-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.
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Cited by
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“SBD possess a b-sheet sandwich to provide a hydrophobic pocket and a a-helices lid (31).”
BackgroundMethodChaperISM: improved chaperone binding prediction using position-independent scoring matrices
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Structural recognition and stabilization of tyrosine hydroxylase by the J-domain protein DNAJC12
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Metadata
- Authors
- Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., & Hendrickson, W. A.
- Venue
- Science
- Published
- 1996-06-14
- Volume
- 272
- Issue
- 5268
- Pages
- 1606-1614
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2076945013
- Cited by
- 1,258
- References
- 0
- FWCI
- 20.90
- Type
- journal article
- Language
- en
- Open access
- green
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