Crystal structure of LacI member, PurR, bound to DNA: Minor groove binding by α helices

Maria A. Schumacher, Kang Yell Choi, Howard Zalkin, Richard G. Brennan

Research output: Contribution to journalArticle

321 Citations (Scopus)

Abstract

The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its compressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 Å resolution by x-ray crystallography. The bipartite structure of PurR consists of an amino-terminal DNA-binding domain and a larger carboxyl-terminal corepressor binding and dimerization domain that is similar to that of the bacterial periplasmic binding proteins. The DNA-binding domain contains a helix-turn-helix motif that makes base-specific contacts in the major groove of the DNA. Base contacts are also made by residues of symmetry-related α helices, the "hinge" helices, which bind deeply in the minor groove. Critical to hinge helix-minor groove binding is the intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54′, into the central CpG-base pair step. These residues thereby act as "leucine levers" to pry open the minor groove and kink the purF operator by 45 degrees.

Original languageEnglish
Pages (from-to)763-770
Number of pages8
JournalScience
Volume266
Issue number5186
DOIs
Publication statusPublished - 1994

All Science Journal Classification (ASJC) codes

  • General

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