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Literature DB >> 3903514

The three-dimensional structure of trp repressor.

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

Abstract

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 near the DNA binding surface.

Entities: Chemical Gene Species

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Year: 1985 PMID： 3903514 DOI： 10.1038/317782a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

73 in total

1. Cooperative folding units of escherichia coli tryptophan repressor.

Authors: A Wallqvist; T A Lavoie; J A Chanatry; D G Covell; J Carey
Journal: Biophys J Date: 1999-09 Impact factor: 4.033

2. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site.

Authors: M A Walsh; Z Otwinowski; A Perrakis; P M Anderson; A Joachimiak
Journal: Structure Date: 2000-05-15 Impact factor: 5.006

The three-dimensional structure of trp repressor.

1. Cooperative folding units of escherichia coli tryptophan repressor.

2. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site.

3. Crystal structure of the Lrp-like transcriptional regulator from the archaeon Pyrococcus furiosus.

4. E. coli trp repressor forms a domain-swapped array in aqueous alcohol.

Review 5. The TetR family of transcriptional repressors.

6. A region of Bacillus subtilis CodY protein required for interaction with DNA.

7. Segmental differences in the stability of the trp-repressor peptide backbone.

8. Sequence-dependent contribution of distal binding domains to CAP protein-DNA binding affinity.

9. High level production and rapid purification of the E. coli trp repressor.

10. Ribosomal protein L7/L12 has a helix-turn-helix motif similar to that found in DNA-binding regulatory proteins.