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Article

Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function.

The EMBO journal - 1 Mar 2001

Sianidis G, Karamanou S, Vrontou E, Boulias K, Repanas K, Kyrpides N, Politou A S, Economou A

Abstract excerpt

SecA, the motor subunit of bacterial polypeptide translocase, is an RNA helicase. SecA comprises a dimerization C-terminal domain fused to an ATPase N-terminal domain containing conserved DEAD helicase motifs. We show that the N-terminal domain is organized like the motor core of DEAD proteins, encompassing two subdomains, NBD1 and IRA2. NBD1, a rigid nucleotide-binding domain, contains the minimal ATPase...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 11230120
DOI: 10.1093/emboj/20.5.961
PMCID: PMC145479

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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