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 during morphogenesis. Although comprised of only 68 residues, it likely interacts 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 determined its solution structure using NMR spectroscopy and have found it to possesses a novel fold consisting of two alpha-helices and a single two-stranded beta-sheet arranged around a well-packed hydrophobic core. The 14 C-terminal residues of gpW, which are essential for function, are unstructured in solution.
Maxwell
K L
KL
Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada.
Yee
A A
AA
Booth
V
V
Arrowsmith
C H
CH
Gold
M
M
Davidson
A R
AR
D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D012996:Solutions; D013816:Thermodynamics; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000378:metabolism
D012996:Solutions; D015678:Viral Structural Proteins; C411883:protein W, bacteriophage lambda