2XGF

Structure of the bacteriophage T4 long tail fibre needle-shaped receptor-binding tip

2XGF の概要

• エントリーDOI: 10.2210/pdb2xgf/pdb
• 分子名称: LONG TAIL FIBER PROTEIN P37, FE (II) ION, CARBONATE ION, ... (4 entities in total)
• 機能のキーワード: viral protein, fiber protein
• 由来する生物種: ENTEROBACTERIA PHAGE T4
• 細胞内の位置: Virion : P03744
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 74439.01

構造登録者

Bartual, S.G.,Otero, J.M.,Garcia-Doval, C.,Llamas-Saiz, A.L.,Kahn, R.,Fox, G.C.,van Raaij, M.J. (登録日: 2010-06-03, 公開日: 2010-11-03, 最終更新日: 2024-05-08)

主引用文献

Bartual, S.G.,Otero, J.M.,Garcia-Doval, C.,Llamas-Saiz, A.L.,Kahn, R.,Fox, G.C.,van Raaij, M.J.
Structure of the bacteriophage T4 long tail fiber receptor-binding tip.
Proc. Natl. Acad. Sci. U.S.A., 107:20287-20292, 2010

PubMed Abstract: Bacteriophages 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.

PubMed: 21041684
DOI: 10.1073/pnas.1011218107

実験手法

X-RAY DIFFRACTION (2.2 Å)