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Article

Study of the ATP-binding site of helicase IV from Escherichia coli.

Biochemical and biophysical research communications - 17 Mar 2006

Dubaele Sandy, Lourdel Claude, Chène Patrick

Abstract excerpt

Helicases contain conserved motifs involved in ATP/magnesium/nucleic acid binding and in the mechanisms coupling nucleotide hydrolysis to duplex unwinding. None of these motifs are located at the adenine-binding pocket of the protein. We show here that the superfamily I helicase, helicase IV from Escherichia coli, utilizes a conserved glutamine and conserved aromatic residue to interact with ATP. Other...

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Identifiers

PMID: 16442499
DOI: 10.1016/j.bbrc.2006.01.040

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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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