2FUG
Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
Summary for 2FUG
Entry DOI | 10.2210/pdb2fug/pdb |
Descriptor | NADH-quinone oxidoreductase chain 1, FE2/S2 (INORGANIC) CLUSTER, FLAVIN MONONUCLEOTIDE, ... (11 entities in total) |
Functional Keywords | oxidoreductase, electron transport, respiratory chain |
Biological source | Thermus thermophilus More |
Cellular location | Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q56222 Q56221 Q56223 Q56220 Q56219 Q56218 Q56224 |
Total number of polymer chains | 32 |
Total formula weight | 1137723.09 |
Authors | Sazanov, L.A.,Hinchliffe, P. (deposition date: 2006-01-26, release date: 2006-02-14, Last modification date: 2024-10-09) |
Primary citation | Sazanov, L.A.,Hinchliffe, P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science, 311:1430-1436, 2006 Cited by PubMed Abstract: Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contains all the redox centers of the enzyme, including nine iron-sulfur clusters. The primary electron acceptor, flavin-mononucleotide, is within electron transfer distance of cluster N3, leading to the main redox pathway, and of the distal cluster N1a, a possible antioxidant. The structure reveals new aspects of the mechanism and evolution of the enzyme. The terminal cluster N2 is coordinated, uniquely, by two consecutive cysteines. The novel subunit Nqo15 has a similar fold to the mitochondrial iron chaperone frataxin, and it may be involved in iron-sulfur cluster regeneration in the complex. PubMed: 16469879DOI: 10.1126/science.1123809 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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