1S3A
NMR Solution Structure of Subunit B8 from Human NADH-Ubiquinone Oxidoreductase Complex I (CI-B8)
Summary for 1S3A
| Entry DOI | 10.2210/pdb1s3a/pdb |
| Descriptor | NADH-ubiquinone oxidoreductase B8 subunit (1 entity in total) |
| Functional Keywords | ci-b8, ndufa2, complex i, oxidoreductase |
| Biological source | Homo sapiens (human) |
| Cellular location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: O43678 |
| Total number of polymer chains | 1 |
| Total formula weight | 11194.87 |
| Authors | Brockmann, C.,Diehl, A.,Rehbein, K.,Kuhne, R.,Oschkinat, H. (deposition date: 2004-01-13, release date: 2005-01-25, Last modification date: 2024-10-30) |
| Primary citation | Brockmann, C.,Diehl, A.,Rehbein, K.,Strauss, H.,Schmieder, P.,Korn, B.,Kuhne, R.,Oschkinat, H. The oxidized subunit B8 from human complex I adopts a thioredoxin fold. Structure, 12:1645-1654, 2004 Cited by PubMed Abstract: Subunit B8 from ubiquinone oxidoreductase (complex I) (CI-B8) is one of several nuclear-encoded supernumerary subunits that are not present in bacterial complex I. Its solution structure shows a thioredoxin fold with highest similarities to the human thioredoxin mutant C73S and thioredoxin 2 from Anabeana sp. Interestingly, these proteins contain active sites in the same area, where the disulfide bond of oxidized CI-B8 is located. The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Analysis of the structure reveals a surface area that is exclusively composed of highly conserved residues and thus most likely a subunit interaction site within complex I. PubMed: 15341729DOI: 10.1016/j.str.2004.06.021 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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