Structure of the TolR periplasmic domain

TolR 周质结构域的结构

• 批准号: 7593497
• 负责人: Ad - Bax
• 金额: $ 21.68万
• 依托单位: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/7593497
• 关键词: Agreement; Binding; Helix (Snails); Knowledge; Maps; Membrane; Numbers; Pattern; Property; Proteins; Residual state; Role; Shapes; Site; Solutions; Structure; Surface; Validation; Vertebral column; Work; base; colicin; ear helix; insight; periplasm; statistics

A NMR study of the solution structure of the TolR periplasmic domain reveals a C2 symmetric homodimer of mixed helix-sheet secondary structure. The structure has been determined on the basis of a large number of interproton NOEs, supplemented by four different types of backbone residual dipolar couplings, including N-H, Ca-Ha, C'-Ca, and N-C'. Reasonable cross validation statistics and good geometric properties attest to the quality of this structure. The shape of the dimeric structure is in excellent agreement with its SAXS diffraction pattern. Work is continuing on defining the colicin interaction site.

对TOLR阴性结构域的溶液结构的NMR研究揭示了混合螺旋式二级结构的C2对称同二聚体。 该结构是基于大量的杂孔NOES确定的，并补充了四种不同类型的骨架残留偶极耦合，包括N-H，Ca-Ha，Ca-Ha，C'-Ca和N-C'。合理的交叉验证统计和良好的几何特性证明了该结构的质量。 二聚体结构的形状与其SAXS衍射模式非常吻合。 工作继续定义结肠素相互作用。