1NEN
Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site
Summary for 1NEN
| Entry DOI | 10.2210/pdb1nen/pdb |
| Descriptor | Succinate dehydrogenase flavoprotein subunit, FE3-S4 CLUSTER, PROTOPORPHYRIN IX CONTAINING FE, ... (15 entities in total) |
| Functional Keywords | membrane protein, respiratory complex, oxidoreductase-electron transport complex, oxidoreductase/electron transport |
| Biological source | Escherichia coli More |
| Cellular location | Cell 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 chains | 4 |
| Total formula weight | 123071.46 |
| 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: 2024-11-13) |
| Primary citation | Yankovskaya, 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: 12560550DOI: 10.1126/science.1079605 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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