6YQ5

Hybrid structure of the SPP1 tail tube by solid-state NMR and cryo EM - NMR Ensemble

6YQ5 の概要

• エントリーDOI: 10.2210/pdb6yq5/pdb
• 関連するPDBエントリー: 6YEG
• EMDBエントリー: 10792
• NMR情報: BMRB: 27468
• 分子名称: Tail tube protein gp17.1* (1 entity in total)
• 機能のキーワード: complex, tail tube, scaffolding, dna transport, viral protein
• 由来する生物種: Bacillus phage SPP1
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 223407.10

構造登録者

Zinke, M.,Sachowsky, K.A.A.,Zinn-Justin, S.,Ravelli, R.,Schroder, G.F.,Habeck, M.,Lange, A. (登録日: 2020-04-16, 公開日: 2020-10-14, 最終更新日: 2024-07-10)

主引用文献

Zinke, M.,Sachowsky, K.A.A.,Oster, C.,Zinn-Justin, S.,Ravelli, R.,Schroder, G.F.,Habeck, M.,Lange, A.
Architecture of the flexible tail tube of bacteriophage SPP1.
Nat Commun, 11:5759-5759, 2020

PubMed Abstract: Bacteriophage SPP1 is a double-stranded DNA virus of the Siphoviridae family that infects the bacterium Bacillus subtilis. This family of phages features a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, we present the atomic structure of the tail tube of phage SPP1. Our hybrid structure is based on the integration of structural restraints from solid-state nuclear magnetic resonance (NMR) and a density map from cryo-EM. We show that the tail tube protein gp17.1 organizes into hexameric rings that are stacked by flexible linker domains and, thus, form a hollow flexible tube with a negatively charged lumen suitable for the transport of DNA. Additionally, we assess the dynamics of the system by combining relaxation measurements with variances in density maps.

PubMed: 33188213
DOI: 10.1038/s41467-020-19611-1

実験手法

ELECTRON MICROSCOPY (4 Å)
SOLID-STATE NMR (4 Å)