Mutants in position 69 of the Trp repressor of Escherichia coli K12 with altered DNA-binding specificity.

doi:10.1007/BF02172524

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Article

Mutants in position 69 of the Trp repressor of Escherichia coli K12 with altered DNA-binding specificity.

Molecular & general genetics : MGG - 12 Jun 1996

Günes C, Müller-Hill B

Abstract excerpt

Structural analysis by X-ray crystallography has indicated that direct contact occurs between Arg69, the second residue of the first helix of the helix-turnhelix (HTH) motif of the Trp repressor, and guanine in position 9 of the alpha-centred consensus trp operator. We therefore replaced residue...

Topics

Amino Acids
Bacterial Proteins
Base Sequence
DNA, Bacterial
DNA-Binding Proteins
Escherichia coli
Helix-Turn-Helix Motifs
Molecular Sequence Data
Mutation
Nucleic Acid Conformation
Operator Regions, Genetic
Repressor Proteins
Sequence Alignment
Thymine
Tryptophan

Source

Open in PubMed

Identifiers

PMID: 8676876
DOI: 10.1007/BF02172524

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8676876-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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