Cited by 145Enzyme Structure and FunctionBacterial Genetics and BiotechnologyProtein Structure and Dynamics

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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Crossref · 10.1038/366178a0

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Citations

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Research works printed but not linked: 3

  1. Luisi, B. F. & Sigler, P. B. Biochem. biophys. Acta 1048, 113–126 (1990).
  2. Roussel, A. & Cambillau, C. in Silicon Graphics Geometry Partner Directory 77–78 (Silicon Graphics, 1989).
  3. Hodel, A., Kim, S.-H. & Brünger, A. T. Acta crystallogr. A. (in the press).

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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
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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CoChat. (2026). Citation check: Tandem binding in crystals of a trp represser/operator half-site complex. https://app.cochat.ai/papers/10.1038/366178a0
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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