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Article

Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.

Protein science : a publication of the Protein Society - 1 Jun 2006

Patel Chetan N, Smith Virginia F, Randall Linda L

Abstract excerpt

The general secretory, Sec, system translocates precursor polypeptides from the cytosol across the cytoplasmic membrane in Escherichia coli. SecB, a small cytosolic chaperone, captures the precursor polypeptides before they fold and delivers them to the membrane translocon through interactions with SecA. Both SecB and SecA display twofold symmetry and yet the complex between the two is stabilized by contacts that...

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Identifiers

PMID: 16731972
DOI: 10.1110/ps.062141006
PMCID: PMC2265093

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.PMID 16731972Read ↗

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