人源线粒体ATP结合盒转运蛋白ABCB7单颗粒冷冻电镜成像数据集

主要面向线粒体内膜膜蛋白三维结构研究。ATP 结合盒亚家族 B 成员 7 (ABCB7) 位于线粒体内膜，在铁代谢中起关键作用。 我们通过单粒子电子冷冻显微镜测定人ABCB7结合不可水解 ATP 类似物腺苷-5'-(β-γ-亚氨基)三磷酸 (AMP-PNP)的复合物 在 3.3 Å分辨率的结构 。 AMP-PNP 结合的人 ABCB7 显示出倒 V 形同源二聚体结构具有向内的开放构象。 在每个单体中鉴定出一个 AMP-PNP 分子和 Mg2+，以及hABCB7 单体的核苷酸结合域 (NBD)。 此外，四种致病的错义突变已映射到该结构，为 X 连锁铁粒幼细胞性贫血和共济失调疾病创建热点图。 我们的研究结果为进一步了解运输机制提供了结构基础。线粒体ABC转运蛋白。

This dataset is primarily targeted at studies on the three-dimensional structures of inner mitochondrial membrane proteins. ATP-binding cassette subfamily B member 7 (ABCB7), which localizes to the inner mitochondrial membrane, plays a critical role in iron metabolism. We determined the structure of the human ABCB7 complex bound to the non-hydrolyzable ATP analog adenosine-5'-(β,γ-imido)triphosphate (AMP-PNP) at 3.3 Å resolution via single-particle cryo-electron microscopy. Human ABCB7 bound with AMP-PNP exhibits an inverted V-shaped homodimeric structure with an inward-open conformation. One AMP-PNP molecule, Mg²+, and the nucleotide-binding domain (NBD) of the hABCB7 monomer were identified in each protomer. Additionally, four pathogenic missense mutations were mapped onto this structure, creating a hotspot map for X-linked sideroblastic anemia and ataxia disorders. Our findings provide a structural basis for further understanding of the transport mechanisms of mitochondrial ABC transporters.

搜集汇总

背景与挑战

背景概述

该数据集利用单颗粒冷冻电镜技术，以3.3 Å分辨率解析了人源线粒体ATP结合盒转运蛋白ABCB7结合AMP-PNP的复合物结构，揭示了其倒V形同源二聚体的开放构象。这一结构研究不仅映射了相关致病突变，还为理解线粒体ABC转运蛋白的运输机制提供了关键基础。