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2FUG

Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus

Summary for 2FUG
Entry DOI10.2210/pdb2fug/pdb
DescriptorNADH-quinone oxidoreductase chain 1, FE2/S2 (INORGANIC) CLUSTER, FLAVIN MONONUCLEOTIDE, ... (11 entities in total)
Functional Keywordsoxidoreductase, electron transport, respiratory chain
Biological sourceThermus thermophilus
More
Cellular locationCell membrane ; Peripheral membrane protein ; Cytoplasmic side : Q56222 Q56221 Q56223 Q56220 Q56219 Q56218 Q56224
Total number of polymer chains32
Total formula weight1137723.09
Authors
Sazanov, L.A.,Hinchliffe, P. (deposition date: 2006-01-26, release date: 2006-02-14, Last modification date: 2024-10-09)
Primary citationSazanov, 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: 16469879
DOI: 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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