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.
Original language | English (US) |
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Pages (from-to) | 782-786 |
Number of pages | 5 |
Journal | Nature |
Volume | 317 |
Issue number | 6040 |
DOIs | |
State | Published - 1985 |
ASJC Scopus subject areas
- General