PMID:9016718
| Citation |
Martínez-Hackert, E and Stock, AM (1997) The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor. Structure 5:109-24 |
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| Abstract |
The differential expression of the ompF and ompC genes is regulated by two proteins that belong to the two component family of signal transduction proteins: the histidine kinase, EnvZ, and the response regulator, OmpR. OmpR belongs to a subfamily of at least 50 response regulators with homologous C-terminal DNA-binding domains of approximately 98 amino acids. Sequence homology with DNA-binding proteins of known structure cannot be detected, and the lack of structural information has prevented understanding of many of this familys functional properties. |
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| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Proteins; Binding Sites; Carbon-Nitrogen Ligases; Conserved Sequence/genetics; Crystallography, X-Ray; DNA-Binding Proteins/chemistry; Escherichia coli/chemistry; Escherichia coli Proteins; Helix-Turn-Helix Motifs; Molecular Sequence Data; Mutagenesis/genetics; Mutation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Repressor Proteins/chemistry; Sequence Alignment; Transcription Factors/chemistry; Transcription, Genetic/genetics |
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