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A proteolytic AAA+ machine poised to unfold a protein substrate.
Ghanbarpour, Alireza; Sauer, Robert T; Davis, Joseph H.
Afiliación
  • Ghanbarpour A; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
  • Sauer RT; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
  • Davis JH; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139.
bioRxiv ; 2023 Dec 15.
Article en En | MEDLINE | ID: mdl-38168193
ABSTRACT
AAA+ proteolytic machines unfold proteins prior to degradation. Cryo-EM of a ClpXP-substrate complex reveals a postulated but heretofore unseen intermediate in substrate unfolding/degradation. The natively folded substrate is drawn tightly against the ClpX channel by interactions between axial pore loops and the substrate degron tail, and by contacts with the native substrate that are, in part, enabled by movement of one ClpX subunit out of the typically observed hexameric spiral.

Texto completo: 1 Bases de datos: MEDLINE Idioma: En Revista: BioRxiv Año: 2023 Tipo del documento: Article

Texto completo: 1 Bases de datos: MEDLINE Idioma: En Revista: BioRxiv Año: 2023 Tipo del documento: Article