...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structure of the lethal phage pinhole
【24h】

Structure of the lethal phage pinhole

机译：致命噬菌体针孔的结构

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Perhaps the simplest of biological timing systems, bacteriophage holins accumulate during the phage morphogenesis period and then trigger to permeabilize the cytoplasmic membrane with lethal holes; thus, terminating the infection cycle. Canonical holins form very large holes that allow nonspecific release of fully-folded proteins, but a recently discovered class of holins, the pinholins, make much smaller holes, or pinholes, that serve only to depolarize the membrane. Here, we interrogate the structure of the prototype pinholin by negative-stain transmission electron-microscopy, cysteine-accessibility, and chemical cross-linking, as well as by computational approaches. Together, the results suggest that the pinholin forms symmetric heptameric structures with the hydro-philic surface of one transmembrane domain lining the surface of a central channel ≈15 A in diameter. The structural model also suggests a rationale for the prehole state of the pinholin, the persistence of which defines the duration of the viral latent period, and for the sensitivity of the holin timing system to the energized state of the membrane.
机译：也许是最简单的生物计时系统，噬菌体孔蛋白在噬菌体形态发生期间积累，然后触发以致死孔透化细胞质膜。因此，终止了感染周期。典型的孔洞形成非常大的孔，从而允许非特异性释放完全折叠的蛋白质，但是最近发现的一类孔洞（品醇）形成了更小的孔或针孔，仅用于使膜去极化。在这里，我们通过负染色透射电子显微镜，半胱氨酸可及性和化学交联以及计算方法来询问原型品的结构。总之，结果表明，品醇溶蛋白形成对称的七聚体结构，其中一个跨膜结构域的亲水表面衬在直径约15 A的中央通道表面上。该结构模型还提出了关于品醇的孔前状态的理论依据，其持续时间定义了病毒潜伏期的持续时间，以及霍林计时系统对膜的激发态的敏感性。

著录项

  • 来源
  • 作者

    Ting Pang; Christos G. Savva; Karen G. Fleming; Douglas K. Struck; Ry Young;

  • 作者单位

    Department of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, TX 77843;

    Microscopy and Imaging Center, Texas A&M University, 2257 TAMU, College Station, TX 77843 Department of Biology, Texas A&M University, 3528 TAMU, College Station, TX 77843;

    Thomas C. Jenkins Department of Biophysics, Johns Hopkins University, 3400 North Charles Street, Baltimore, MA 21218;

    Department of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, TX 77843;

    Department of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, TX 77843;

  • 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

    glycine zipper; holin; lysis; SAR domain; thiol modification;

    机译：甘氨酸拉链霍林裂解SAR域;硫醇修饰;

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号