Structural variation in PWWP domains

J Mol Biol. 2003 Jul 11;330(3):571-6. doi: 10.1016/s0022-2836(03)00470-4.

Abstract

The PWWP domain is a ubiquitous eukaryotic protein module characterised by a region of sequence similarity of approximately 80 amino acids containing a highly conserved PWWP motif. It is frequently found in proteins associated with chromatin. We have determined the structure of a PWWP domain from the S. pombe protein SPBC215.07c using NMR spectroscopy. The structure is composed of a five stranded beta barrel followed by two alpha helices. Comparison to the recently reported structure of a homologous domain from the mammalian DNA methyltransferase Dnmt3b reveals substantial differences both in the C-terminal helical region and in the PWWP motif.

MeSH terms

  • Amino Acid Sequence
  • Conserved Sequence
  • DNA (Cytosine-5-)-Methyltransferases / chemistry
  • DNA Methyltransferase 3B
  • Hydrophobic and Hydrophilic Interactions
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Tertiary*
  • Schizosaccharomyces pombe Proteins / chemistry*
  • Schizosaccharomyces pombe Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Structural Homology, Protein

Substances

  • SPBC215.O7C protein, S pombe
  • Schizosaccharomyces pombe Proteins
  • DNA (Cytosine-5-)-Methyltransferases

Associated data

  • PDB/1H3Z