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Literature DB >> 3600756

The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity.

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

Abstract

Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking alpha-helices from both subunits.

Entities: Chemical Gene

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Year: 1987 PMID： 3600756 DOI： 10.1038/327591a0

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

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Cited

59 in total

1. Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.

Authors: L H Weaver; K Kwon; D Beckett; B W Matthews
Journal: Proc Natl Acad Sci U S A Date: 2001-05-15 Impact factor: 11.205

2. The effect of selective deuteration on magnetization transfer in larger proteins.

Authors: R Pachter; C H Arrowsmith; O Jardetzky
Journal: J Biomol NMR Date: 1992-03 Impact factor: 2.835

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

Authors: Catherine L Lawson; Brian Benoff; Tatyana Berger; Helen M Berman; Jannette Carey
Journal: Structure Date: 2004-06 Impact factor: 5.006

4. NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution.

Authors: E Liepinsh; G Otting; K Wüthrich
Journal: Nucleic Acids Res Date: 1992-12-25 Impact factor: 16.971

The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity.

1. Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.

2. The effect of selective deuteration on magnetization transfer in larger proteins.

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

4. NMR observation of individual molecules of hydration water bound to DNA duplexes: direct evidence for a spine of hydration water present in aqueous solution.

5. Preliminary crystallography confirms that the archaeal DNA-binding and tryptophan-sensing regulator TrpY is a dimer.

6. Synthesis of an enzymatically active FLP recombinase in vitro: search for a DNA-binding domain.

7. NikR-operator complex structure and the mechanism of repressor activation by metal ions.

8. Conformational changes necessary for gene regulation by Tet repressor assayed by reversible disulfide bond formation.

9. Rapid corepressor exchange from the trp-repressor/operator complex: an NMR study of [ul-13C/15N]-L-tryptophan.

10. Visualization of trp repressor and its complexes with DNA by atomic force microscopy.