DNA recognition by GAL4: structure of a protein-DNA complex - PubMed (original) (raw)

. 1992 Apr 2;356(6368):408-14.

doi: 10.1038/356408a0.

Affiliations

• PMID: 1557122
• DOI: 10.1038/356408a0

DNA recognition by GAL4: structure of a protein-DNA complex

R Marmorstein et al. Nature. 1992.

Abstract

A specific DNA complex of the 65-residue, N-terminal fragment of the yeast transcriptional activator, GAL4, has been analysed at 2.7 A resolution by X-ray crystallography. The protein binds as a dimer to a symmetrical 17-base-pair sequence. A small, Zn(2+)-containing domain recognizes a conserved CCG triplet at each end of the site through direct contacts with the major groove. A short coiled-coil dimerization element imposes 2-fold symmetry. A segment of extended polypeptide chain links the metal-binding module to the dimerization element and specifies the length of the site. The relatively open structure of the complex would allow another protein to bind coordinately with GAL4.

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Comment in

• DNA transcription. Zinc standard for economy.
  Luisi B. Luisi B. Nature. 1992 Apr 2;356(6368):379-80. doi: 10.1038/356379a0. Nature. 1992. PMID: 1557114 No abstract available.

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