1qo8

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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qo8 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qo8 ConSurf].
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== Publication Abstract from PubMed ==
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Fumarate reductases and succinate dehydrogenases play central roles in the metabolism of eukaryotic and prokaryotic cells. A recent medium resolution structure of the Escherichia coli fumarate reductase (Frd) has revealed the overall organization of the membrane-bound complex. Here we present the first high resolution X-ray crystal structure of a water-soluble bacterial fumarate reductase in an open conformation. This structure reveals a mobile domain that modulates substrate access to the active site and provides new insights into the mechanism of this widespread and important family of FAD-containing respiratory proteins.
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Open conformation of a flavocytochrome c3 fumarate reductase.,Bamford V, Dobbin PS, Richardson DJ, Hemmings AM Nat Struct Biol. 1999 Dec;6(12):1104-7. PMID:10581549<ref>PMID:10581549</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
*[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]]
*[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]]
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== References ==
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<references/>
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</StructureSection>
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Current revision

The structure of the open conformation of a flavocytochrome c3 fumarate reductase

PDB ID 1qo8

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