2fbw: Difference between revisions

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New page: left|200px<br /><applet load="2fbw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fbw, resolution 2.10Å" /> '''Avian respiratory co...
 
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==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Succinate dehydrogenase (ubiquinone)]]
[[Category: Succinate dehydrogenase (ubiquinone)]]
[[Category: Anderson, V.E.]]
[[Category: Anderson, V E.]]
[[Category: Berry, E.A.]]
[[Category: Berry, E A.]]
[[Category: Cobessi, D.]]
[[Category: Cobessi, D.]]
[[Category: Huang, L.S.]]
[[Category: Huang, L S.]]
[[Category: Shen, J.T.]]
[[Category: Shen, J T.]]
[[Category: Sun, G.]]
[[Category: Sun, G.]]
[[Category: Tung, E.Y.]]
[[Category: Tung, E Y.]]
[[Category: Wang, A.C.]]
[[Category: Wang, A C.]]
[[Category: AZI]]
[[Category: AZI]]
[[Category: BHG]]
[[Category: BHG]]
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[[Category: respiratory chain]]
[[Category: respiratory chain]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:45 2008''

Revision as of 18:19, 21 February 2008

File:2fbw.gif


2fbw, resolution 2.10Å

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Avian respiratory complex II with carboxin bound

OverviewOverview

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.

About this StructureAbout this Structure

2FBW is a Protein complex structure of sequences from Gallus gallus with , , , , , , , , , , , and as ligands. Active as Succinate dehydrogenase (ubiquinone), with EC number 1.3.5.1 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

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