- EMDB-34225: cryo-EM structure of the human respiratory complex II -
+
Open data
ID or keywords:
Loading...
-
Basic information
Entry
Database: EMDB / ID: EMD-34225
Title
cryo-EM structure of the human respiratory complex II
Map data
Sample
Complex: The human mitochondrial complex II, composed of SDHA, SDHB, SDHC and SDHD
Protein or peptide: x 4 types
Ligand: x 7 types
Keywords
succinate dehydrogenase / electron transport chain / human mitochondria / OXIDOREDUCTASE / oxidative phosphorylation
Function / homology
Function and homology information
regulation of catecholamine secretion / succinate metabolic process / Oxidoreductases; Acting on the CH-OH group of donors; With a quinone or similar compound as acceptor / succinate dehydrogenase activity / : / mitochondrial electron transport, succinate to ubiquinone / Citric acid cycle (TCA cycle) / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / Maturation of TCA enzymes and regulation of TCA cycle ...regulation of catecholamine secretion / succinate metabolic process / Oxidoreductases; Acting on the CH-OH group of donors; With a quinone or similar compound as acceptor / succinate dehydrogenase activity / : / mitochondrial electron transport, succinate to ubiquinone / Citric acid cycle (TCA cycle) / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / Maturation of TCA enzymes and regulation of TCA cycle / Respiratory electron transport / mitochondrial envelope / 3 iron, 4 sulfur cluster binding / proton motive force-driven mitochondrial ATP synthesis / ubiquinone binding / tricarboxylic acid cycle / aerobic respiration / respiratory electron transport chain / mitochondrial membrane / 2 iron, 2 sulfur cluster binding / nervous system development / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / cellular response to hypoxia / mitochondrial inner membrane / electron transfer activity / heme binding / nucleolus / mitochondrion / nucleoplasm / membrane / metal ion binding / plasma membrane Similarity search - Function
National Natural Science Foundation of China (NSFC)
81520108019, 813300237,32100976,82222042
China
Chinese Academy of Sciences
2017YFC0840300,2020YFA0707500
China
Citation
Journal: Proc Natl Acad Sci U S A / Year: 2023 Title: Structure of the human respiratory complex II. Authors: Zhanqiang Du / Xiaoting Zhou / Yuezheng Lai / Jinxu Xu / Yuying Zhang / Shan Zhou / Ziyan Feng / Long Yu / Yanting Tang / Weiwei Wang / Lu Yu / Changlin Tian / Ting Ran / Hongming Chen / ...Authors: Zhanqiang Du / Xiaoting Zhou / Yuezheng Lai / Jinxu Xu / Yuying Zhang / Shan Zhou / Ziyan Feng / Long Yu / Yanting Tang / Weiwei Wang / Lu Yu / Changlin Tian / Ting Ran / Hongming Chen / Luke W Guddat / Fengjiang Liu / Yan Gao / Zihe Rao / Hongri Gong / Abstract: Human complex II is a key protein complex that links two essential energy-producing processes: the tricarboxylic acid cycle and oxidative phosphorylation. Deficiencies due to mutagenesis have been ...Human complex II is a key protein complex that links two essential energy-producing processes: the tricarboxylic acid cycle and oxidative phosphorylation. Deficiencies due to mutagenesis have been shown to cause mitochondrial disease and some types of cancers. However, the structure of this complex is yet to be resolved, hindering a comprehensive understanding of the functional aspects of this molecular machine. Here, we have determined the structure of human complex II in the presence of ubiquinone at 2.86 Å resolution by cryoelectron microscopy, showing it comprises two water-soluble subunits, SDHA and SDHB, and two membrane-spanning subunits, SDHC and SDHD. This structure allows us to propose a route for electron transfer. In addition, clinically relevant mutations are mapped onto the structure. This mapping provides a molecular understanding to explain why these variants have the potential to produce disease.
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)
EMDB accession codes are about to change! (news from PDBe EMDB page)
The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
The EM Navigator/Yorodumi systems omit the EMD- prefix.
Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator
Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.
Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi