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Article

Mutational analysis of the helicase-like domain of Thermotoga maritima reverse gyrase.

The Journal of biological chemistry - 10 Oct 2008

de la Tour Claire Bouthier, Amrani Laila, Cossard Raynald, Neuman Keir C, Serre Marie Claude, Duguet Michel

Abstract excerpt

Reverse gyrase is a unique type IA topoisomerase that is able to introduce positive supercoils into DNA in an ATP-dependent process. ATP is bound to the helicase-like domain of the enzyme that contains most of the conserved motifs found in helicases of the SF1 and SF2 superfamilies. In this paper, we have investigated the role of the conserved helicase motifs I, II, V, VI, and Q by generating mutants of the...

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Source

Identifiers

PMID: 18614530
DOI: 10.1074/jbc.M800867200

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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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Mutational analysis of the helicase-like domain of Thermotoga maritima reverse gyrase.PMID 18614530Read ↗

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