Motor mechanism of native ATPase complexes

天然 ATP 酶复合物的运动机制

• 批准号: 122511187
• 负责人: Professorin Dr. Petra Wendler
• 金额: --
• 依托单位: Institut für Biochemie und Biologie
• 依托单位国家: 德国
• 项目类别: Independent Junior Research Groups
• 财政年份: 2009
• 资助国家: 德国
• 起止时间: 2008-12-31 至 2014-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/122511187?language=en
• 关键词: Motor; mechanism; native; ATPase; complexes

ATPases of the AAA+ superfamily (ATPases associated with various cellular activities) are often at the core of multi-protein complexes responsible for timely destruction or remodeling of macromolecules in an energy dependent manner. They form one of the largest protein superfamilies and are crucial components in most re-organization and recycling processes of protein, membrane or DNA within the cell. Their unique functional specificity derives from combining the highly conserved AAA+ domain with accessory domains and proteins which facilitate fine tuning of the AAA+ activity. The goal of this project is to determine the three dimensional structure of different functional AAA+ assemblies in order to understand the common underlying mechanism of action of AAA+ proteins and its regulation by accessory factors. Using single particle cryo electron microscopy the functional states of (i) heat shock protein (Hsp) 100 variants with varying sized domain insertions, (ii) proteasomal subcomplexes and (iii) hetero oligomeric peroxisomal ATPase assemblies will be explored.

AAA+超家族的ATP酶（与各种细胞活动相关的ATP酶）通常是多蛋白复合物的核心，负责以能量依赖的方式及时破坏或重塑大分子。它们构成了最大的蛋白质超家族之一，并且是细胞内蛋白质、膜或 DNA 的大多数重组和回收过程的关键组成部分。它们独特的功能特异性源自高度保守的 AAA+ 结构域与辅助结构域和蛋白质的结合，有助于微调 AAA+ 活性。该项目的目标是确定不同功能 AAA+ 组装体的三维结构，以了解 AAA+ 蛋白的共同潜在作用机制及其受辅助因子的调节。使用单颗粒冷冻电子显微镜，将探索 (i) 具有不同大小结构域插入的热休克蛋白 (Hsp) 100 变体、(ii) 蛋白酶体亚复合物和 (iii) 异源寡聚过氧化物酶体 ATP 酶组件的功能状态。