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Article

Quaternary dynamics of the SecA motor drive translocase catalysis.

Molecular cell - 12 Dec 2013

Gouridis Giorgos, Karamanou Spyridoula, Sardis Marios Frantzeskos, Schärer Martin Alexander, Capitani Guido, Economou Anastassios

Abstract excerpt

Most secretory preproteins exit bacterial cells through the protein translocase, comprising the SecYEG channel and the dimeric peripheral ATPase motor SecA. Energetic coupling to work remains elusive. We now demonstrate that translocation is driven by unusually dynamic quaternary changes in SecA. The dimer occupies several successive states with distinct protomer arrangements. SecA docks on SecYEG as a dimer and...

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Source

Identifiers

PMID: 24332176
DOI: 10.1016/j.molcel.2013.10.036

Provenance

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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Quaternary dynamics of the SecA motor drive translocase catalysis.PMID 24332176Read ↗

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