德国马克斯·普朗克生物物理研究所Werner Kühlbrandt和Lea Dietrich共同合作，近期取得重要工作进展。他们研究发现在整细胞条件下，Polytomella线粒体ATP合酶的原位结构与旋转状态。相关研究成果2024年9月6日在线发表于《科学》杂志上。

据介绍，细胞依赖于三磷酸腺苷（ATP）这种通用能源货币的持续供应。在线粒体中，ATP是通过一系列氧化还原反应产生的，从而在线粒体内膜上建立电化学梯度。ATP合酶利用梯度的能量从二磷酸腺苷（ADP）和无机磷酸盐中产生ATP。

研究人员通过电子低温断层扫描和平均分辨率高达4.2埃的亚图谱确定了单细胞鞭毛虫Polytomella线粒体内ATP合酶的结构，揭示了中央柄的六个旋转位置，分为F1头部的21个亚态。Polytomella ATP合酶形成具有多个相邻行的螺旋阵列，这些行定义了嵴。在膜电位存在下，ATP合酶在天然操作条件下的结构是原位分析膜蛋白复合物的关键一步。

附：英文原文

Title: In situ structure and rotary states of mitochondrial ATP synthase in whole Polytomella cells

Author: Lea Dietrich, Ahmed-Noor A. Agip, Christina Kunz, Andre Schwarz, Werner Kühlbrandt

Issue&Volume: 2024-09-06

Abstract: Cells depend on a continuous supply of adenosine triphosphate (ATP), the universal energy currency. In mitochondria, ATP is produced by a series of redox reactions, whereby an electrochemical gradient is established across the inner mitochondrial membrane. The ATP synthase harnesses the energy of the gradient to generate ATP from adenosine diphosphate (ADP) and inorganic phosphate. We determined the structure of ATP synthase within mitochondria of the unicellular flagellate Polytomella by electron cryo-tomography and subtomogram averaging at up to 4.2-angstrom resolution, revealing six rotary positions of the central stalk, subclassified into 21 substates of the F1 head. The Polytomella ATP synthase forms helical arrays with multiple adjacent rows defining the cristae ridges. The structure of ATP synthase under native operating conditions in the presence of a membrane potential represents a pivotal step toward the analysis of membrane protein complexes in situ.

DOI: adp4640

Source: https://www.science.org/doi/10.1126/science.adp4640