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

• Published in: Journal of molecular biology Vol. 308; no. 1; pp. 9 - 14
• Main Authors: Maxwell, Karen L, Yee, Adelinda A, Booth, Valerie, Arrowsmith, Cheryl H, Gold, Marvin, Davidson, Alan R
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 20.04.2001
• Subjects: Amino Acid Sequence; Bacteriophage lambda - chemistry; bacteriophage λ; connector; glycoprotein W; head morphogenesis; Models, Molecular; Molecular Sequence Data; NMR structure; Nuclear Magnetic Resonance, Biomolecular; Phage l; Protein Folding; Protein Structure, Quaternary; Protein Structure, Secondary; protein W; Sequence Alignment; Solutions; Thermodynamics; Viral Structural Proteins - chemistry; Viral Structural Proteins - metabolism; bacteriophage λ; NMR structure; connector; NOE; protein W; gp; head morphogenesis
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1006/jmbi.2001.4582

Protein W (gpW) from bacteriophage λ 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 α-helices and a single two-stranded β-sheet arranged around a well-packed hydrophobic core. The 14 C-terminal residues of gpW, which are essential for function, are unstructured in solution.