4osd

Publication Abstract from PubMed

Gene product 5 (gp5) of bacteriophage T4 is a spike-shaped protein that functions to disrupt the membrane of the target cell during phage infection. Its C-terminal domain is a long and slender beta-helix that is formed by three polypeptide chains wrapped around a common symmetry axis akin to three interdigitated corkscrews. The folding and biophysical properties of such triple-stranded beta-helices, which are topologically related to amyloid fibers, represent an unsolved biophysical problem. Here, we report structural and biophysical characterization of T4 gp5 beta-helix and its truncated mutants of different lengths. A soluble fragment that forms a dimer of trimers and that could comprise a minimal self-folding unit has been identified. Surprisingly, the hydrophobic core of the beta-helix is small. It is located near the C-terminal end of the beta-helix and contains a centrally positioned and hydrated magnesium ion. A large part of the beta-helix interior comprises a large elongated cavity that binds palmitic, stearic, and oleic acids in an extended conformation suggesting that these molecules might participate in the folding of the complete beta-helix.

Structure and Biophysical Properties of a Triple-Stranded Beta-Helix Comprising the Central Spike of Bacteriophage T4.,Buth SA, Menin L, Shneider MM, Engel J, Boudko SP, Leiman PG Viruses. 2015 Aug 18;7(8):4676-706. doi: 10.3390/v7082839. PMID:26295253^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.