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Crystal Structure of LacI Member, PurR, Bound to DNA: Minor Groove Binding by α Helices

Schumacher, Maria A., Choi, Kang Yell, Zalkin, Howard, Brennan, Richard G.·1994·Science

Abstract

The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, 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 Leu 54 and its symmetry-related mate, Leu 54′ , 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.

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Metadata

Authors
Schumacher, M. A., Choi, K. Y., Zalkin, H., & Brennan, R. G.
Venue
Science
Published
1994-11-04
Volume
266
Issue
5186
Pages
763-770
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2072920810
Cited by
371
References
1
FWCI
19.19
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Crystal Structure of LacI Member, PurR, Bound to DNA: Minor Groove Binding by α Helices. https://app.cochat.ai/papers/10.1126/science.7973627
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Schumacher, M. A., Choi, K. Y., Zalkin, H., & Brennan, R. G. (1994). Crystal Structure of LacI Member, PurR, Bound to DNA: Minor Groove Binding by α Helices. Science. https://doi.org/10.1126/science.7973627

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