A new DNA-binding motif in the Skn-1 binding domain-DNA complex

Nat Struct Biol. 1998 Jun;5(6):484-91. doi: 10.1038/nsb0698-484.

Abstract

The DNA-binding domain of Skn-1, a developmental transcription factor that specifies mesoderm in C. elegans, is shown by X-ray crystallography to have a novel fold in which a compact, monomeric, four-helix unit organizes two DNA-contact elements. At the C-terminus, a helix extends from the domain to occupy the major groove of DNA in a manner similar to bZip proteins. Skn-1, however, lacks the leucine zipper found in all bZips. Additional contacts with the DNA are made by a short basic segment at the N-terminus of the domain, reminiscent of the 'homeodomain arm'.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Composition
  • Caenorhabditis elegans / chemistry*
  • Caenorhabditis elegans / embryology
  • Caenorhabditis elegans Proteins*
  • Conserved Sequence
  • Crystallography, X-Ray
  • DNA / chemistry
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / genetics
  • Dimerization
  • Fungal Proteins / chemistry
  • Helminth Proteins / chemistry*
  • Helminth Proteins / genetics
  • Homeodomain Proteins / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Nucleic Acid Conformation
  • Protein Folding
  • Protein Kinases / chemistry
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid
  • Transcription Factors / chemistry

Substances

  • Caenorhabditis elegans Proteins
  • DNA-Binding Proteins
  • Fungal Proteins
  • Helminth Proteins
  • Homeodomain Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • skn-1 protein, C elegans
  • DNA
  • Protein Kinases

Associated data

  • PDB/1SKN