Mechanics of Hsp70 chaperones enables differential interaction with client proteins
Hsp70 chaperones interact with many proteins through a substrate-trapping mechanism that requires ATP. Hsp70s have a lid over the substrate-binding cleft, whose function is controversial. Using cysteine cross-linking and EPR in the Escherichia coli Hsp70 DnaK, it is now shown that helix B of the lid...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
30 January 2011
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| In: |
Nature structural & molecular biology
Year: 2011, Volume: 18, Issue: 3, Pages: 345-351 |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb.2006 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/nsmb.2006 Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/nsmb.2006 
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| Author Notes: | Rainer Schlecht, Annette H. Erbse, Bernd Bukau & Matthias P. Mayer |
| Summary: | Hsp70 chaperones interact with many proteins through a substrate-trapping mechanism that requires ATP. Hsp70s have a lid over the substrate-binding cleft, whose function is controversial. Using cysteine cross-linking and EPR in the Escherichia coli Hsp70 DnaK, it is now shown that helix B of the lid subdomain can adopt three major conformational states and that it does not necessarily close over bound substrates, allowing binding of natively folded states. |
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| Item Description: | Gesehen am 12.10.2022 |
| Physical Description: | Online Resource |
| ISSN: | 1545-9985 |
| DOI: | 10.1038/nsmb.2006 |