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

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

Research output: Contribution to journalArticlepeer-review

216 Scopus citations

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 α-helices from both subunits.

Original languageEnglish (US)
Pages (from-to)591-597
Number of pages7
JournalNature
Volume327
Issue number6123
DOIs
StatePublished - 1987

ASJC Scopus subject areas

  • General

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