The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Tandem binding in crystals of a trp represser/operator half-site complex
Abstract
The crystal structure of trp repressor tandemly bound in a 2:1 complex to a 16-base-pair palindromic DNA containing a central trp operator half-site has been determined and refined to 2.4 A resolution. Despite dramatically different DNA sequence contexts and crystallization conditions, the protein/DNA interface is essentially identical to that seen in the original trp repressor/operator complex structure. Water-mediated sequence recognition by trp repressor is likely to be related to the unusual end-on approach of the recognition helix (E), which allows sharing of the major groove by tandem dimers. The tandem complex model accounts for the mutational sensitivity of all trp operator base pairs. The structure also provides the first detailed view of the tandem interaction, revealing a key role for the amino-terminal arms.
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“The two Fur dimers are positioned on almost opposite sides of the double helix, in contrast to the positioning of other prokaryotic helix-turn-helix motif class repressors, such as the trp repressor 41 .”
From Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator (2015) · cites this paper as [41]
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Structure of the metal-ion-activated diphtheria toxin repressor/ tox operator complex
White, A., Ding, X., vanderSpek, J. C., Murphy, J. R., & Ringe, D. (1998) · Nature · doi:10.1038/28893 · Cited by 180
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Metadata
- Authors
- Lawson, C. L., & Carey, J.
- Affiliations
- Brookhaven National Laboratory (US)
- Princeton University (US)
- Venue
- Nature
- Published
- 1993-11
- Volume
- 366
- Issue
- 6451
- Pages
- 178-182
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1997329250
- Cited by
- 145
- References
- 31
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2020: 2 · 2018: 1 · 2017: 1 · 2015: 3 · 2014: 1 · 2012: 1
- FWCI
- 18.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- trp repressor, protein-DNA interface, palindromic DNA, recognition helix, major groove, transcriptional repression, DNA sequence recognition
- MeSH terms
- Bacterial Proteins, Base Sequence, Computer Graphics, DNA, Bacterial, Escherichia coli, Models, Molecular, Molecular Sequence Data, Operator Regions, Genetic, Protein Binding, Repressor Proteins, Crystallography, X-Ray, Escherichia coli Proteins
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- Lawson, C. L., & Carey, J. (1993). Tandem binding in crystals of a trp represser/operator half-site complex. Nature. https://doi.org/10.1038/366178a0