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Article

A tightly regulated molecular toggle controls AAA+ disaggregase.

Nature structural & molecular biology - 1 Dec 2012

Oguchi Yuki, Kummer Eva, Seyffer Fabian, Berynskyy Mykhaylo, Anstett Benjamin, Zahn Regina, Wade Rebecca C, Mogk Axel, Bukau Bernd

Abstract excerpt

The ring-forming AAA+ protein ClpB cooperates with the DnaK chaperone system to refold aggregated proteins in Escherichia coli. The M domain, a ClpB-specific coiled-coil structure with two wings, motif 1 and motif 2, is essential to disaggregation, but the positioning and mechanistic role of M domains in ClpB hexamers remain unresolved. We show that M domains nestle at the ClpB ring surface, with both M-domain...

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PMID: 23160353
DOI: 10.1038/nsmb.2441

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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A tightly regulated molecular toggle controls AAA+ disaggregase.PMID 23160353Read ↗

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