2fug
From Proteopedia
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Crystal structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
Overview
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.
About this Structure
2FUG is a Protein complex structure of sequences from Thermus thermophilus with SF4, FES and FMN as ligands. Active as NADH dehydrogenase (quinone), with EC number 1.6.99.5 Full crystallographic information is available from OCA.
Reference
Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus., Sazanov LA, Hinchliffe P, Science. 2006 Mar 10;311(5766):1430-6. Epub 2006 Feb 9. PMID:16469879
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