Crystal structure of trp represser/operator complex at atomic resolution

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

Research output: Contribution to journalArticlepeer-review

798 Scopus citations


The crystal structure of the trp repressor/operator complex shows an extensive contact surface, including 24 direct and 6 solvent-mediated hydrogen bonds to the phosphate groups of the DNA. There are no direct hydrogen bonds or non-polar contacts to the bases that can explain the repressor's specificity for the operator sequence. Rather, the sequence seems to be recognized indirectly through its effects on the geometry of the phosphate backbone, which in turn permits the formation of a stable interface. Water-mediated polar contacts to the bases also appear to contribute part of the specificity.

Original languageEnglish (US)
Pages (from-to)321-329
Number of pages9
Issue number6188
StatePublished - 1988

ASJC Scopus subject areas

  • General


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