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Article

Intradomain LexA rotation is a prerequisite for DNA binding specificity.

FEBS letters - 16 Oct 2007

Butala Matej, Hodoscek Milan, Anderluh Gregor, Podlesek Zdravko, Zgur-Bertok Darja

Abstract excerpt

In the absence of DNA damage the LexA protein represses the bacterial SOS system. We performed molecular dynamic simulations of two LexA dimers bound to operators. Our model predicted that rotation of the LexA DNA binding domain, with respect to the dimerised C-terminal domain, is required for selective DNA binding. To confirm the model, double and quadruple cysteine LexA mutants were engineered. Electrophoretic...

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Source

Identifiers

PMID: 17884043
DOI: 10.1016/j.febslet.2007.09.006

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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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