Structural variation in PWWP domains.
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.
Slater
Leanne M
LM
MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 2QH, UK.
Allen
Mark D
MD
Bycroft
Mark
M
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D004248:DNA (Cytosine-5-)-Methyltransferases / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein; D000097584:DNA Methyltransferase 3B
D004248:DNA (Cytosine-5-)-Methyltransferases; D029702:Schizosaccharomyces pombe Proteins; D000097584:DNA Methyltransferase 3B; C476221:SPBC215.O7C protein, S pombe