Structure of mammalian respirasome
详细信息 查看官网全文
- 英文论文题名：Structure of mammalian respirasome
- 论文作者：Runyu Guo
- 英文论文作者：Runyu Guo ; Beijing Advanced Innovation Center for Structural Biology ; School of Life Sciences ; Tsinghua University
- 年：2016
- 作者机构：Beijing Advanced Innovation Center for Structural Biology,School of Life Sciences,Tsinghua University;
- 英文论文关键词：Cellular respiration ; Respiratory chain ; Respirasome ; Supercomplex organization
- 会议召开时间：2016-12-19
- 会议录名称：中国晶体学会第六届学术年会暨会员代表大会（大分子晶体学分会）论文摘要集
- 英文会议录名称：Abstracts of the 6th Annual Conference of Chinese Crystallographic Society
- 语种：英文
- 分类号：Q952
- 学会代码：ZGJY
- 会议名称：中国晶体学会第六届学术年会暨会员代表大会（大分子晶体学分会）
- 会议地点：中国广东广州
- 主办单位：中国晶体学会
- 学会名称：中国晶体学会
- 页数：1
- 文件大小：111k
- 原文格式：D
- 会议级别：全国
摘要
Cellular respiration is the most fundamental biological process in almost all living creatures,thus becoming the central research focus of physiological mechanism and medical care.Various protein complexes are identified to catalyse specific steps of cellular respiration,and furthermore these protein complexes are considered to function as an integrity,which is called respiratory supercomplexes,or respirasome.In different organisms,different combinations of individual respiratory complexes are preferred,and even in the same organism,the combinations can vary with cell conditions,leading to the so-called plastic model.According to the latest structures of respirasome,many cutting-edge discussions about the mechanism of electron transfer and the assembly process of protein complexes are raised.The respiratory chain complexes I,III and IV(CI,CIII,and CIV) exist in the bacterial membrane or the inner mitochondrial membrane(IMM) to transfer electrons and to establish the proton gradient for ATP synthesis by complex V.The respiratory chain complexes can assemble into supercomplexes(SCs),but their precise arrangement is unknown.Here,we report a 5.4-? cryo-electron microscopy(EM) structure of the major 1.7-MDa SCI1III2IV1(respirasome) purified from porcine heart.The CIII dimer and CIV bind at the same side of the L-shaped CI,with their transmembrane(TM) domains virtually aligned to form a TM disk.Compared to free CI,the CI in the respirasome is more compact,owing to interactions with CIII and CIV.The supernumerary components,NDUFA11 and NDUFB9,contribute to the oligomerization of CI and CIII.Together,the structure of the respirasome provides the precise arrangements of the respiratory chain complexes in mitochondria.
Cellular respiration is the most fundamental biological process in almost all living creatures,thus becoming the central research focus of physiological mechanism and medical care.Various protein complexes are identified to catalyse specific steps of cellular respiration,and furthermore these protein complexes are considered to function as an integrity,which is called respiratory supercomplexes,or respirasome.In different organisms,different combinations of individual respiratory complexes are preferred,and even in the same organism,the combinations can vary with cell conditions,leading to the so-called plastic model.According to the latest structures of respirasome,many cutting-edge discussions about the mechanism of electron transfer and the assembly process of protein complexes are raised.The respiratory chain complexes I,III and IV(CI,CIII,and CIV) exist in the bacterial membrane or the inner mitochondrial membrane(IMM) to transfer electrons and to establish the proton gradient for ATP synthesis by complex V.The respiratory chain complexes can assemble into supercomplexes(SCs),but their precise arrangement is unknown.Here,we report a 5.4-? cryo-electron microscopy(EM) structure of the major 1.7-MDa SCI1III2IV1(respirasome) purified from porcine heart.The CIII dimer and CIV bind at the same side of the L-shaped CI,with their transmembrane(TM) domains virtually aligned to form a TM disk.Compared to free CI,the CI in the respirasome is more compact,owing to interactions with CIII and CIV.The supernumerary components,NDUFA11 and NDUFB9,contribute to the oligomerization of CI and CIII.Together,the structure of the respirasome provides the precise arrangements of the respiratory chain complexes in mitochondria.
Cellular respiration is the most fundamental biological process in almost all living creatures,thus becoming the central research focus of physiological mechanism and medical care.Various protein complexes are identified to catalyse specific steps of cellular respiration,and furthermore these protein complexes are considered to function as an integrity,which is called respiratory supercomplexes,or respirasome.In different organisms,different combinations of individual respiratory complexes are preferred,and even in the same organism,the combinations can vary with cell conditions,leading to the so-called plastic model.According to the latest structures of respirasome,many cutting-edge discussions about the mechanism of electron transfer and the assembly process of protein complexes are raised.The respiratory chain complexes I,III and IV(CI,CIII,and CIV) exist in the bacterial membrane or the inner mitochondrial membrane(IMM) to transfer electrons and to establish the proton gradient for ATP synthesis by complex V.The respiratory chain complexes can assemble into supercomplexes(SCs),but their precise arrangement is unknown.Here,we report a 5.4-? cryo-electron microscopy(EM) structure of the major 1.7-MDa SCI1III2IV1(respirasome) purified from porcine heart.The CIII dimer and CIV bind at the same side of the L-shaped CI,with their transmembrane(TM) domains virtually aligned to form a TM disk.Compared to free CI,the CI in the respirasome is more compact,owing to interactions with CIII and CIV.The supernumerary components,NDUFA11 and NDUFB9,contribute to the oligomerization of CI and CIII.Together,the structure of the respirasome provides the precise arrangements of the respiratory chain complexes in mitochondria.
引文