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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of the DNA-recognition component of the bacterial virus Sf6 genome-packaging machine
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Crystal structure of the DNA-recognition component of the bacterial virus Sf6 genome-packaging machine

机译：细菌病毒Sf6基因组​​包装机的DNA识别组件的晶体结构

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摘要

In herpesviruses and many bacterial viruses, genome-packaging is a precisely mediated process fulfilled by a virally encoded molecular machine called terminase that consists of two protein components: A DNA-recognition component that defines the specificity for packaged DNA, and a catalytic component that provides energy for the packaging reaction by hydrolyzing ATP. The terminase docks onto the portal protein complex embedded in a single vertex of a preformed viral protein shell called procapsid, and pumps the viral DNA into the procapsid through a conduit formed by the portal. Here we report the 1.65 A resolution structure of the DNA-recognition component gp1 of the Shigella bacteriophage Sf6 genome-packaging machine. The structure reveals a ring-like octamer formed by interweaved protein monomers with a highly extended fold, embracing a tunnel through which DNA may be translocated. The N-terminal DNA-binding domains form the peripheral appendages surrounding the octamer. The central domain contributes to oligomerization through interactions of bundled helices. The C-terminal domain forms a barrel with parallel beta-strands. The structure reveals a common scheme for oligomerization of terminase DNA-recognition components, and provides insights into the role of gp1 in formation of the packaging-competent terminase complex and assembly of the terminase with the portal, in which ring-like protein oligomers stack together to form a continuous channel for viral DNA translocation.
机译：在疱疹病毒和许多细菌病毒中，基因组包装是由称为末端酶的病毒编码分子机器完成的精确介导的过程，该机器由两个蛋白质成分组成：一个DNA识别成分，定义了包装DNA的特异性；一个催化成分，提供了通过水解ATP为包装反应提供能量。末端酶对接在门户蛋白复合物上，该门户蛋白复合物嵌在预先形成的病毒蛋白壳（称为衣壳）的单个顶点中，并通过门户形成的导管将病毒DNA泵入衣壳。在这里，我们报告了志贺氏菌噬菌体Sf6基因组​​包装机的DNA识别组件gp1的1.65 A解析结构。该结构揭示了由交织的蛋白质单体形成的环状八聚体，具有高度延伸的折叠，包围着可通过其进行DNA转运的通道。 N末端DNA结合结构域形成围绕八聚体的外围附件。中央结构域通过成束螺旋的相互作用促进低聚。 C末端结构域形成具有平行β链的桶。该结构揭示了末端酶DNA识别组件寡聚的通用方案，并提供了gp1在具有包装能力的末端酶复合物的形成以及末端酶与门的组装中的作用的见解，其中环状蛋白寡聚体堆叠在一起形成病毒DNA易位的连续通道。

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  • 作者

    Haiyan Zhao; Casey J. Finch; Reuben D. Sequeira; Brian A. Johnson; John E. Johnson; Sherwood R. Casjens; Liang Tang;

  • 作者单位

    Department of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, KS 66045;

    rnDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, KS 66045;

    rnDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, KS 66045;

    rnDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, KS 66045;

    rnDepartment of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037;

    rnDepartment of Pathology, University of Utah Medical School, Salt Lake City, UT 84112;

    rnDepartment of Molecular Biosciences, University of Kansas, 1200 Sunnyside Avenue, Lawrence, KS 66045;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    terminase; DNA-packaging; oligomer; bacteriophage; protein:DNA interaction;

    机译：末端酶DNA包装;低聚物噬菌体蛋白质：DNA相互作用;

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