2fug

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

Structural highlights 2fug is a 32 chain structure with sequence from Thermus thermophilus HB8. The December 2011 RCSB PDB Molecule of the Month feature on Complex I by David Goodsell is 10.2210/rcsb_pdb/mom_2011_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NQO2_THET8 NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient required for the synthesis of ATP. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also NADH-quinone oxidoreductase

spinqualitylabelsall models 2fug, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image