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研究解析ATP合酶四聚体冷冻电镜结构
作者:小柯机器人 发布时间:2019/7/19 12:34:27

近日,清华大学杨茂君(Maojun Yang)课题组的研究通过冷冻电镜技术,解析了结合IF1抑制蛋白的ATP合酶四聚体的结构。 2019年6月14日出版的《科学》发表了这项成果。

该课题组分离了猪四聚腺苷三磷酸合成酶,用单粒子低温电子显微镜对其结构进行了6.2埃分辨率的解析。从矩阵上看,两个经典的v型ATP合酶二聚体相互平行,形成一个h型ATP合酶四聚体。ATP合酶抑制因子亚单位1 (IF1)是一种已知的低pH条件下哺乳动物ATP合酶的体内抑制剂。两个IF1二聚体连接两个ATP合酶二聚体,与处于抑制状态的ATP合酶四聚体一致。在四聚体中,课题组研究人员解析了两种不同旋转构象的完整ATP合酶3.34埃和3.45埃结构。

据悉,线粒体三磷酸腺苷合成酶(ATP)产生哺乳动物细胞所需的大部分ATP。
 

附:英文原文

Title: Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1

Author: Jinke Gu, Laixing Zhang, Shuai Zong, Runyu Guo, Tianya Liu, Jingbo Yi, Peiyi Wang, Wei Zhuo, Maojun Yang

Issue&Volume:VOL 364, ISSUE 6445,14 JUNE 2019

Abstract: The mitochondrial adenosine triphosphate (ATP) synthase produces most of the ATP required by mammalian cells. We isolated porcine tetrameric ATP synthase and solved its structure at 6.2-angstrom resolution using a single-particle cryo–electron microscopy method. Two classical V-shaped ATP synthase dimers lie antiparallel to each other to form an H-shaped ATP synthase tetramer, as viewed from the matrix. ATP synthase inhibitory factor subunit 1 (IF1) is a well-known in vivo inhibitor of mammalian ATP synthase at low pH. Two IF1 dimers link two ATP synthase dimers, which is consistent with the ATP synthase tetramer adopting an inhibited state. Within the tetramer, we refined structures of intact ATP synthase in two different rotational conformations at 3.34- and 3.45-Å resolution.

DOI: DOI: 10.1126/science.aaw4852

Source: https://science.sciencemag.org/content/364/6445/1068

期刊信息
Science:《科学》,创刊于1880年。隶属于美国科学促进会,最新IF:41.037