The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold

Protein W (gpW) from bacteriophage lambda is required for the stabilization of DNA within the phage head and for attachment of tails onto the head dur ing morphogenesis. Although comprised of only 68 residues, it likely intera cts with at least two other proteins in the mature phage and with DNA. Thus , gpW is an intriguing subject for detailed structural studies. We have det ermined its solution structure using NMR spectroscopy and have found it to possesses a novel fold consisting of two alpha -helices and a single two-st randed beta -sheet arranged around a well-packed hydrophobic core. The 14 C -terminal residues of gpW, which are essential for function, are unstructur ed in solution. (C) 2001 Academic Press.