A common fold mediates vertebrate defense and bacterial attack

Protein crystallography raw diffraction images and unmerged reflection intensities Collection size: 36.1 GB Number of datasets: 5 Citation: Rosado et. al. (2007) A common fold mediates vertebrate defense and bacterial attack. Science. In Press. Proteins containing membrane attack complex/perforin (MACPF) domains play important roles in vertebrate immunity, embryonic development, and neural-cell migration. In vertebrates, the ninth component of complement and perforin form oligomeric pores that lyse bacteria and kill virus-infected cells, respectively. However, the mechanism of MACPF function is unknown. We determined the crystal structure of a bacterial MACPF protein, Plu-MACPF from Photorhabdus luminescens, to 2.0 angstrom resolution. The MACPF domain reveals structural similarity with poreforming cholesterol-dependent cytolysins (CDCs) from Gram-positive bacteria. This suggests that lytic MACPF proteins may use a CDC-like mechanism to form pores and disrupt cell membranes. Sequence similarity between bacterial and vertebrate MACPF domains suggests that the fold of the CDCs, a family of proteins important for bacterial pathogenesis, is probably used by vertebrates for defense against infection. To cite this data use the following DOI: 10.4225/52/557F9B41BBAC7

蛋白质晶体学原始衍射图像与未合并反射强度
集合大小：36.1 GB
数据集数量：5
引用文献：Rosado等人（2007）。一种通用折叠介导脊椎动物防御与细菌攻击。《科学》，待发表。
含有膜攻击复合物/穿孔素（MACPF）结构域的蛋白质在脊椎动物免疫、胚胎发育及神经细胞迁移中发挥重要作用。在脊椎动物中，补体第九成分与穿孔素分别形成寡聚孔道，裂解细菌并杀死病毒感染细胞。然而，MACPF的功能机制尚不清楚。我们解析了来自发光光杆状菌（Photorhabdus luminescens）的细菌MACPF蛋白Plu-MACPF的晶体结构，分辨率达2.0埃。MACPF结构域与革兰氏阳性菌中形成孔道的胆固醇依赖性细胞溶素（CDC）具有结构相似性。这表明溶血性MACPF蛋白可能采用类似CDC的机制形成孔道并破坏细胞膜。细菌与脊椎动物MACPF结构域之间的序列相似性表明，对细菌致病机制（pathogenesis）至关重要的CDC家族蛋白的折叠方式，可能被脊椎动物用于抵御感染。
引用本数据请使用以下DOI：10.4225/52/557F9B41BBAC7