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Article

Structure of dimeric SecA, the Escherichia coli preprotein translocase motor.

Journal of molecular biology - 9 Mar 2007

Papanikolau Yannis, Papadovasilaki Maria, Ravelli Raimond B G, McCarthy Andrew A, Cusack Stephen, Economou Anastassios, Petratos Kyriacos

Abstract excerpt

SecA is the preprotein translocase ATPase subunit and a superfamily 2 (SF2) RNA helicase. Here we present the 2 A crystal structures of the Escherichia coli SecA homodimer in the apo form and in complex with ATP, ADP and adenosine 5'-[beta,gamma-imido]triphosphate (AMP-PNP). Each monomer contains the SF2 ATPase core (DEAD motor) built of two domains (nucleotide binding domain, NBD and intramolecular regulator of...

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Share to Adenosine Diphosphate
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Share to Crystallography, X-Ray

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Source

Identifiers

PMID: 17229438
DOI: 10.1016/j.jmb.2006.12.049

Genes

PNP

Provenance

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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Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

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