5BU5

HK620 Tail Needle crystallized at pH 9 (crystal form I)

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5BU5 の概要

• エントリーDOI: 10.2210/pdb5bu5/pdb
• 関連するPDBエントリー: 5BU8
• 分子名称: DNA stabilization protein, CHLORIDE ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: tail needle, viral genome-ejection, coiled-coil, trimer, bacteriophage, viral protein
• 由来する生物種: Enterobacteria phage HK620
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 150659.77

構造登録者

Bhardwaj, A.,Cingolani, G. (登録日: 2015-06-03, 公開日: 2015-06-24, 最終更新日: 2023-09-27)

主引用文献

Bhardwaj, A.,Sankhala, R.S.,Olia, A.S.,Brooke, D.,Casjens, S.R.,Taylor, D.J.,Prevelige, P.E.,Cingolani, G.
Structural Plasticity of the Protein Plug That Traps Newly Packaged Genomes in Podoviridae Virions.
J.Biol.Chem., 291:215-226, 2016

PubMed Abstract: Bacterial viruses of the P22-like family encode a specialized tail needle essential for genome stabilization after DNA packaging and implicated in Gram-negative cell envelope penetration. The atomic structure of P22 tail needle (gp26) crystallized at acidic pH reveals a slender fiber containing an N-terminal "trimer of hairpins" tip. Although the length and composition of tail needles vary significantly in Podoviridae, unexpectedly, the amino acid sequence of the N-terminal tip is exceptionally conserved in more than 200 genomes of P22-like phages and prophages. In this paper, we used x-ray crystallography and EM to investigate the neutral pH structure of three tail needles from bacteriophage P22, HK620, and Sf6. In all cases, we found that the N-terminal tip is poorly structured, in stark contrast to the compact trimer of hairpins seen in gp26 crystallized at acidic pH. Hydrogen-deuterium exchange mass spectrometry, limited proteolysis, circular dichroism spectroscopy, and gel filtration chromatography revealed that the N-terminal tip is highly dynamic in solution and unlikely to adopt a stable trimeric conformation at physiological pH. This is supported by the cryo-EM reconstruction of P22 mature virion tail, where the density of gp26 N-terminal tip is incompatible with a trimer of hairpins. We propose the tail needle N-terminal tip exists in two conformations: a pre-ejection extended conformation, which seals the portal vertex after genome packaging, and a postejection trimer of hairpins, which forms upon its release from the virion. The conformational plasticity of the tail needle N-terminal tip is built in the amino acid sequence, explaining its extraordinary conservation in nature.

PubMed: 26574546
DOI: 10.1074/jbc.M115.696260

実験手法

X-RAY DIFFRACTION (1.952 Å)