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Article

The three-dimensional structure of trp repressor.

Nature - 1 Jan 2000

Schevitz R W, Otwinowski Z, Joachimiak A, Lawson C L, Sigler P B

Abstract excerpt

The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution. The dimeric protein has a remarkable subunit interface in which five of each subunit's six helices are interlinked. The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix-turn-helix motif and by moulding the details of the repressor's structure...

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Identifiers

PMID: 3903514
DOI: 10.1038/317782a0

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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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