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E. coli trp repressor forms a domain-swapped array in aqueous alcohol
The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA-binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 Å X-ray structure o...
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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2004
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3228604/ https://ncbi.nlm.nih.gov/pubmed/15274929 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2004.03.019 |
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