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Literature DB >> 28220774

Proteasomes, caught in the act.

Abstract

Although energy-dependent protein destruction by the proteasome has been known for over 30 years, how this intricate molecular machine uses ATP to power protein degradation has remained very poorly understood. In a recently published paper, Ding et al. present a snapshot of the proteasome mid-catalysis, yielding new and unexpected insights into the catalytic mechanism of this ATP-powered multisubunit machine.

Entities: Chemical Gene

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Year: 2017 PMID： 28220774 PMCID： PMC5339839 DOI： 10.1038/cr.2017.22

Source DB: PubMed Journal: Cell Res ISSN： 1001-0602 Impact factor: 25.617

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References

10 in total

1. Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis.

Authors: Anne S Meyer; Joel R Gillespie; Dirk Walther; Ian S Millet; Sebastian Doniach; Judith Frydman
Journal: Cell Date: 2003-05-02 Impact factor: 41.582

Review 2. Structure and function of the AAA+ nucleotide binding pocket.

Authors: Petra Wendler; Susanne Ciniawsky; Malte Kock; Sebastian Kube
Journal: Biochim Biophys Acta Date: 2011-07-28

3. Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation.

Authors: Paweł Śledź; Pia Unverdorben; Florian Beck; Günter Pfeifer; Andreas Schweitzer; Friedrich Förster; Wolfgang Baumeister
Journal: Proc Natl Acad Sci U S A Date: 2013-04-15 Impact factor: 11.205

Proteasomes, caught in the act.

1. Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis.

Review 2. Structure and function of the AAA+ nucleotide binding pocket.

3. Structure of the 26S proteasome with ATP-γS bound provides insights into the mechanism of nucleotide-dependent substrate translocation.

4. An atomic structure of the human 26S proteasome.

5. Nucleotide binding and conformational switching in the hexameric ring of a AAA+ machine.

6. Structure of the human 26S proteasome at a resolution of 3.9 Å.

7. The hexameric helicase DnaB adopts a nonplanar conformation during translocation.

8. Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase.

9. ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function.

10. Conformational switching of the 26S proteasome enables substrate degradation.