细菌鞭毛马达单颗粒冷冻电镜成像数据集

细菌鞭毛运动是一种超分子蛋白机器，驱动鞭毛旋转运动，这是细菌在不同环境中生存至关重要的，也是致病性的关键决定因素。鞭毛运动的详细结构尚不清楚。在这里，我们提出了一个原子分辨率的低温电子显微镜(cryo-EM)结构的细菌鞭毛马达与钩的复合物，由175个亚基组成，分子质量约为6.3MDa。结构表明，10个从MS环突出FlgB和FliE亚基的肽介导了MS环向棒的扭矩传递，克服了电机旋转结构和螺旋结构之间的对称不匹配。低压环接触远端杆，并施加静电力来支持其旋转和扭矩传输到钩子。这项工作提供了详细的分子见解的结构，组装，和扭矩传递机制的鞭毛马达。

Bacterial flagellar motility is a supramolecular protein machine that drives flagellar rotation, which is crucial for bacterial survival in diverse environments and a key determinant of pathogenicity. The precise architecture of the flagellar motor remains elusive. Here, we report the atomic-resolution cryo-electron microscopy (cryo-EM) structure of the bacterial flagellar motor-hook complex, which comprises 175 subunits with a molecular mass of approximately 6.3 MDa. The structure demonstrates that 10 peptides from FlgB and FliE subunits protruding from the MS ring mediate torque transmission from the MS ring to the rod, resolving the symmetry mismatch between the rotary motor architecture and the helical structure. The low-pressure ring contacts the distal rod and exerts electrostatic forces to support its rotation and torque transmission to the hook. This work provides detailed molecular insights into the structure, assembly, and torque transmission mechanisms of the bacterial flagellar motor.

搜集汇总

背景与挑战

背景概述

该数据集提供了细菌鞭毛马达与钩复合物的原子分辨率冷冻电镜结构，该结构由175个亚基组成，分子质量约为6.3MDa。研究揭示了马达中扭矩传递的详细分子机制，为理解鞭毛马达的组装和功能提供了关键见解。