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Structure of the bacteriophage T4 long tail fibre needle-shaped receptor-binding tipStructure of the bacteriophage T4 long tail fibre needle-shaped receptor-binding tip
Structural highlights
FunctionFIB37_BPT4 Structural component of the distal-half of the long-tail fiber. It constitutes the part of the long-tail fibers that recognizes the bacterial receptor. The long-tail fiber of T4 is about 1600 Angstroms long with a kink in the middle that divides the fiber into proximal and distal halves. The thin tip of the distal half-fiber interacts with the bacterial lipopolysaccharide receptor and specifies the host range of the phage.[1] Publication Abstract from PubMedBacteriophages are the most numerous organisms in the biosphere. In spite of their biological significance and the spectrum of potential applications, little high-resolution structural detail is available on their receptor-binding fibers. Here we present the crystal structure of the receptor-binding tip of the bacteriophage T4 long tail fiber, which is highly homologous to the tip of the bacteriophage lambda side tail fibers. This structure reveals an unusual elongated six-stranded antiparallel beta-strand needle domain containing seven iron ions coordinated by histidine residues arranged colinearly along the core of the biological unit. At the end of the tip, the three chains intertwine forming a broader head domain, which contains the putative receptor interaction site. The structure reveals a previously unknown beta-structured fibrous fold, provides insights into the remarkable stability of the fiber, and suggests a framework for mutations to expand or modulate receptor-binding specificity. Structure of the bacteriophage T4 long tail fiber receptor-binding tip.,Bartual SG, Otero JM, Garcia-Doval C, Llamas-Saiz AL, Kahn R, Fox GC, van Raaij MJ Proc Natl Acad Sci U S A. 2010 Nov 1. PMID:21041684[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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