...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Membrane assembly of M13 major coat protein: Evidence for a structural adaptation in the hinge region and a tilted transmembrane domain
【24h】

Membrane assembly of M13 major coat protein: Evidence for a structural adaptation in the hinge region and a tilted transmembrane domain

机译：M13主要外壳蛋白的膜组件：在铰链区和倾斜的跨膜结构域的结构适应的证据。

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

New insights into the low-resolution Structure of the hinge region and the transmembrane domain of the membrane-bound major coat protein of the bacteriophage M13 are deduced from a single cysteine-scanning approach using fluorescence spectroscopy. New mutant coat proteins are labeled and reconstituted into phospholipid bilayers with varying headgroup compositions (PC, PE, and PG) and thicknesses (14:1PC, 18:1PC, and 22:1PC). Information about the polarity of the local environment around the labeled sites is deduced from the wavelength of maximum emission using AEDANS attached to the SH groups of the cysteines as a fluorescent probe. It is found that the protein is almost entirely embedded in the membrane, whereas the phospholipid headgroup composition of the membrane hardly affects the overall embedment of the protein in the membrane. From the assessment of a hydrophobic and hydrophilic face of the transmembrane helix, it is concluded that the helix is tilted with respect to the membrane normal. As compared to the thicker 18:1PC and 22:1PC membranes, reconstitution of the protein in the thin 14:1PC membranes results in a loss of helical structure and in the formation of a stretched conformation of the hinge region. It is suggested that the hinge region acts as a flexible spring between the N-terminal amphipathic arm and transmembrane hydrophobic helix. On average, the membrane-bound state of the coat protein can be seen as a gently curved and tilted, "banana-shaped" molecule, which is strongly anchored in the membrane-water interface at the C-terminus. From our experiments, we propose a rather small conformational adaptation of the major coat protein as the most likely reversible mechanism for responding to environmental changes during the bacteriophage disassembly and assembly process.
机译：从单一的半胱氨酸扫描方法，使用荧光光谱法可以得出对噬菌体M13的膜结合主要外壳蛋白的铰链区和跨膜结构域的低分辨率结构的新见解。标记了新的突变外壳蛋白，并重组为具有不同头基组成（PC，PE和PG）和厚度（14：1PC，18：1PC和22：1PC）的磷脂双层。使用连接到半胱氨酸的SH基团的AEDANS作为荧光探针，可从最大发射波长推导有关标记位置周围局部环境极性的信息。已发现蛋白质几乎完全包埋在膜中，而膜的磷脂头基组成几乎不影响蛋白质在膜中的整体包埋。根据对跨膜螺旋的疏水和亲水面的评估，可以得出结论，该螺旋相对于膜法线倾斜。与较厚的18：1PC和22：1PC膜相比，薄的14：1PC膜中蛋白质的重建导致螺旋结构的丧失和铰链区拉伸构象的形成。建议铰链区充当N末端两亲臂和跨膜疏水螺旋之间的弹性弹簧。平均而言，外壳蛋白的膜结合状态可以看作是一个柔和弯曲和倾斜的“香蕉形”分子，该分子牢固地锚定在C端的膜-水界面中。从我们的实验中，我们提出主要外壳蛋白的构象适应性很小，这是在噬菌体拆卸和组装过程中响应环境变化的最可能的可逆机制。

著录项

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