2fbw: Difference between revisions

Revision as of 10:21, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fbw.png

Template:STRUCTURE 2fbw

Avian respiratory complex II with carboxin boundAvian respiratory complex II with carboxin bound

Template:ABSTRACT PUBMED 16371358

About this StructureAbout this Structure

2FBW is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

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., Huang LS, Sun G, Cobessi D, Wang AC, Shen JT, Tung EY, Anderson VE, Berry EA, J Biol Chem. 2006 Mar 3;281(9):5965-72. Epub 2005 Dec 21. PMID:16371358

Page seeded by OCA on Tue Jul 29 10:21:06 2008

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OCA

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-'''Avian respiratory complex II with carboxin bound'''
+===Avian respiratory complex II with carboxin bound===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16371358}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Redox enzyme]]
 [[Category: Respiratory chain]]
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