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呼吸复合体IV的冷冻电镜结构

Cryo-EM structure of respiratory complex IV.

作者信息

Bausewein Thomas, Nussberger Stephan, Kühlbrandt Werner

机构信息

Department of Structural Biology, Max-Planck-Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany.

Abteilung Biophysik, Institut für Biomaterialien und biomolekulare Systeme, Universität Stuttgart, Pfaffenwaldring 57, 70550 Stuttgart, Germany.

出版信息

IUCrJ. 2019 Jun 26;6(Pt 4):773-780. doi: 10.1107/S2052252519007486. eCollection 2019 Jul 1.

Abstract

In fungi, the mitochondrial respiratory chain complexes (complexes I-IV) are responsible for oxidative phosphorylation, as in higher eukaryotes. Cryo-EM was used to identify a 200 kDa membrane protein from in lipid nanodiscs as cytochrome oxidase (complex IV) and its structure was determined at 5.5 Å resolution. The map closely resembles the cryo-EM structure of complex IV from . Its ten subunits are conserved in and , but other transmembrane subunits are missing. The different structure of the Cox5a subunit is typical for fungal complex IV and may affect the interaction with complex III in a respiratory supercomplex. Additional density was found between the matrix domains of the Cox4 and Cox5a subunits that appears to be specific to .

摘要

在真菌中,线粒体呼吸链复合物(复合物I-IV)与高等真核生物一样,负责氧化磷酸化。冷冻电镜用于从脂质纳米盘中鉴定出一种200 kDa的膜蛋白作为细胞色素c氧化酶(复合物IV),并在5.5 Å分辨率下确定了其结构。该图谱与来自[具体物种]的复合物IV的冷冻电镜结构非常相似。其十个亚基在[具体物种1]和[具体物种2]中是保守的,但其他跨膜亚基缺失。Cox5a亚基的不同结构是真菌复合物IV的典型特征,可能会影响其在呼吸超级复合物中与复合物III的相互作用。在Cox4和Cox5a亚基的基质结构域之间发现了额外的密度,这似乎是[具体物种]特有的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/01f3/6608615/ff363ab318a7/m-06-00773-fig1.jpg

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