首页|Pentameric Assembly Architecture of the Tail Tube Protein in SPR Phages

Pentameric Assembly Architecture of the Tail Tube Protein in SPR Phages

扫码查看
原文链接
  • 万方数据
  • 维普
Most phages—viruses infecting prokaryotes—inject their genomes via a tail structure.The central tail tube,composed of tail tube protein(TTP),typically forms conserved hexameric or trimeric rings.In this paper,we report a novel pentameric TTP assembly,solved by cryo-electron microscopy(cryo-EM)at 3.5 Å and 3.7 Å resolution.Structural analysis reveals a highly negatively charged inner surface of this pentameric tube.Key residues in the loop connecting β3 and β4 strands are crucial for pentameric ring formation.Mismatches in interactions between stacked layers can induce curvature in the tube.The cryo-EM structure of the TTP polymer at the tube's end shows that β-strands spanning amino acids 27-65 shift toward the central tunnel,potentially obstructing the passage of the phage genome.This study provides new structural insights into a unique TTP assembly,enhancing our understanding of phage assembly processes.

Lin Wang、Yuhang He、Kaixiang Zhu、Sheng Cui、Xiaopan Gao、Kun Shang、Hongtao Zhu

展开 >

Beijing National Laboratory for Condensed Matter Physics and Laboratory of Soft Matter Physics,Institute of Physics,Chinese Academy of Sciences,Beijing 100190,China

Medical School,Yan'an University,Yan'an 716099,China

NHC Key Laboratory of Systems Biology of Pathogens,National Institute of Pathogen Biology,Chinese Academy of Medical Sciences and Peking Union Medical College,Beijing 102629,China

University of Chinese Academy of Sciences,Beijing 100049,China

Songshan Lake Materials Laboratory,Dongguan 523830,China

展开 >

2024

10.1088/0256-307X/41/12/128701

中国物理快报(英文版)
中国科学院物理研究所,中国物理学会

中国物理快报(英文版)

CSTPCDEI
影响因子：0.515
ISSN：0256-307X
年,卷(期)：2024.41(12)