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

被引：156

作者：

Gu, Jinke ^{[1
]}

Zhang, Laixing ^{[1
]}

Zong, Shuai ^{[1
]}

Guo, Runyu ^{[1
]}

Liu, Tianya ^{[1
]}

Yi, Jingbo ^{[1
]}

Wang, Peiyi ^{[2
]}

Zhuo, Wei ^{[1
]}

Yang, Maojun ^{[1
,3
]}

机构：

[1] Tsinghua Univ, Sch Life Sci, Beijing Adv Innovat Ctr Struct Biol, Minist Educ,Key Lab Prot Sci,Tsinghua Peking Join, Beijing 100084, Peoples R China

[2] Southern Univ Sci & Technol, SUSTech CryoEM Facil Ctr, Shenzhen 518055, Peoples R China

[3] Huazhong Univ Sci & Technol, Sch Pharm, Tongji Med Coll, Wuhan 430030, Hubei, Peoples R China

来源：

SCIENCE | 2019年 / 364卷 / 6445期

基金：

国家重点研发计划; 中国博士后科学基金; 中国国家自然科学基金;

关键词：

INNER MITOCHONDRIAL-MEMBRANE; BEAM-INDUCED MOTION; REGULATORY PROTEIN; F-1-ATPASE; RESOLUTION; ARCHITECTURE; SUBUNIT; CRISTAE; DOMAIN; ORGANIZATION;

D O I：

10.1126/science.aaw4852

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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-angstrom resolution.

引用

页码：1068 / +

页数：52

共 67 条

[1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].