1YQ3

Avian respiratory complex ii with oxaloacetate and ubiquinone

Summary for 1YQ3

• Entry DOI: 10.2210/pdb1yq3/pdb
• Related: 1YQ4
• Descriptor: Succinate dehydrogenase flavoprotein subunit, FE3-S4 CLUSTER, Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer, ... (16 entities in total)
• Functional Keywords: complex ii, membrane protein, heme protein, iron sulfur protein, cytochrome b, oxidoreductase, redox enzyme, respiratory chain, oxaloacetate ubiquinone
• Biological source: Gallus gallus (chicken); More
• Cellular location: Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side : Q9YHT1 Q9YHT2; Mitochondrion inner membrane ; Multi-pass membrane protein : Q5ZIS0
• Total number of polymer chains: 4
• Total formula weight: 128412.08

Authors

Huang, L.,Cobessi, D.,Tung, E.Y.,Berry, E.A. (deposition date: 2005-02-01, release date: 2005-12-20, Last modification date: 2023-08-23)

Primary citation

Huang, L.,Sun, G.,Cobessi, D.,Wang, A.C.,Shen, J.T.,Tung, E.Y.,Anderson, V.E.,Berry, E.A.
3-Nitropropionic Acid Is a Suicide Inhibitor of Mitochondrial Respiration That, upon Oxidation by Complex II, Forms a Covalent Adduct with a Catalytic Base Arginine in the Active Site of the Enzyme
J.Biol.Chem., 281:5965-5972, 2006

PubMed Abstract: We report three new structures of mitochondrial respiratory Complex II (succinate ubiquinone oxidoreductase, E.C. 1.3.5.1) at up to 2.1 A resolution, with various inhibitors. The structures define the conformation of the bound inhibitors and suggest the residues involved in substrate binding and catalysis at the dicarboxylate site. In particular they support the role of Arg(297) as a general base catalyst accepting a proton in the dehydrogenation of succinate. The dicarboxylate ligand in oxaloacetate-containing crystals appears to be the same as that reported for Shewanella flavocytochrome c treated with fumarate. The plant and fungal toxin 3-nitropropionic acid, an irreversible inactivator of succinate dehydrogenase, forms a covalent adduct with the side chain of Arg(297). The modification eliminates a trypsin cleavage site in the flavoprotein, and tandem mass spectroscopic analysis of the new fragment shows the mass of Arg(297) to be increased by 83 Da and to have the potential of losing 44 Da, consistent with decarboxylation, during fragmentation.

PubMed: 16371358
DOI: 10.1074/jbc.M511270200

Experimental method

X-RAY DIFFRACTION (2.2 Å)