Mechanics of Hsp70 chaperones enables differential interaction with client proteins

• Verfasst von: Schlecht, Rainer [VerfasserIn]
• Verfasst von: Erbse, Annette [VerfasserIn]
• Verfasst von: Bukau, Bernd [VerfasserIn]
• Verfasst von: Mayer, Matthias P. [VerfasserIn]
• Titel: Mechanics of Hsp70 chaperones enables differential interaction with client proteins
• Verf.angabe: Rainer Schlecht, Annette H. Erbse, Bernd Bukau & Matthias P. Mayer
• E-Jahr: 2011
• Jahr: 30 January 2011
• Umfang: 7 S.
• Fussnoten: Gesehen am 12.10.2022
• Titel Quelle: Enthalten in: Nature structural & molecular biology
• Ort Quelle: London [u.a.] : Nature Publishing Group, 2004
• Jahr Quelle: 2011
• Band/Heft Quelle: 18(2011), 3, Seite 345-351
• ISSN Quelle: 1545-9985
• DOI: doi:10.1038/nsmb.2006
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Chaperones
• Sach-SW: Structural biology
• K10plus-PPN: 181877190X

Abstract

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.