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1NEK

Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound

Summary for 1NEK
Entry DOI10.2210/pdb1nek/pdb
Related1nen
DescriptorSuccinate dehydrogenase flavoprotein subunit, FE3-S4 CLUSTER, PROTOPORPHYRIN IX CONTAINING FE, ... (15 entities in total)
Functional Keywordsmembrane protein, oxygen respiratory chain, oxidoreductase-electron transport complex, oxidoreductase/electron transport
Biological sourceEscherichia coli
More
Cellular locationCell inner membrane; Peripheral membrane protein; Cytoplasmic side: P0AC41
Cell inner membrane; Peripheral membrane protein: P07014
Cell inner membrane; Multi-pass membrane protein: P69054 P0AC44
Total number of polymer chains4
Total formula weight123107.58
Authors
Yankovskaya, V.,Horsefield, R.,Tornroth, S.,Luna-Chavez, C.,Miyoshi, H.,Leger, C.,Byrne, B.,Cecchini, G.,Iwata, S. (deposition date: 2002-12-11, release date: 2003-02-25, Last modification date: 2024-11-20)
Primary citationYankovskaya, V.,Horsefield, R.,Tornroth, S.,Luna-Chavez, C.,Miyoshi, H.,Leger, C.,Byrne, B.,Cecchini, G.,Iwata, S.
Architecture of succinate dehydrogenase and reactive oxygen species generation.
Science, 299:700-704, 2003
Cited by
PubMed Abstract: The structure of Escherichia coli succinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron donor, succinate, to the terminal electron acceptor, ubiquinone. It was found that the SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species (ROS) formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of ROS. Furthermore, symptoms of genetic disorders associated with mitochondrial SQR mutations may be a result of ROS formation resulting from impaired electron transport in the enzyme.
PubMed: 12560550
DOI: 10.1126/science.1079605
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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