1fcd
From Proteopedia
(New page: 200px<br /><applet load="1fcd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fcd, resolution 2.53Å" /> '''THE STRUCTURE OF FLA...) |
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| - | [[Image:1fcd.gif|left|200px]]<br /><applet load="1fcd" size=" | + | [[Image:1fcd.gif|left|200px]]<br /><applet load="1fcd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fcd, resolution 2.53Å" /> | caption="1fcd, resolution 2.53Å" /> | ||
'''THE STRUCTURE OF FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE FROM A PURPLE PHOTOTROPHIC BACTERIUM CHROMATIUM VINOSUM AT 2.5 ANGSTROMS RESOLUTION'''<br /> | '''THE STRUCTURE OF FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE FROM A PURPLE PHOTOTROPHIC BACTERIUM CHROMATIUM VINOSUM AT 2.5 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase | + | The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit. The diheme cytochrome folds as two domains, each resembling mitochondrial cytochrome c, and has an unusual interpropionic acid linkage joining the two heme groups in the interior of the subunit. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. A tryptophan, threonine, or tyrosine side chain may provide a partial conduit for electron transfer to one of the heme groups located 10 angstroms from the flavin. |
==About this Structure== | ==About this Structure== | ||
| - | 1FCD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum] with FAD and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FCD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FCD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Allochromatium vinosum]] | [[Category: Allochromatium vinosum]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bartsch, R | + | [[Category: Bartsch, R G.]] |
| - | [[Category: Beeumen, J | + | [[Category: Beeumen, J J.Van.]] |
| - | [[Category: Chen, Z | + | [[Category: Chen, Z W.]] |
| - | [[Category: Cusanovich, M | + | [[Category: Cusanovich, M A.]] |
| - | [[Category: Driessche, G | + | [[Category: Driessche, G Van.]] |
[[Category: Koh, M.]] | [[Category: Koh, M.]] | ||
| - | [[Category: Mathews, F | + | [[Category: Mathews, F S.]] |
| - | [[Category: Meyer, T | + | [[Category: Meyer, T E.]] |
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: electron transport(flavocytochrome)]] | [[Category: electron transport(flavocytochrome)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:13 2008'' |
Revision as of 10:37, 21 February 2008
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THE STRUCTURE OF FLAVOCYTOCHROME C SULFIDE DEHYDROGENASE FROM A PURPLE PHOTOTROPHIC BACTERIUM CHROMATIUM VINOSUM AT 2.5 ANGSTROMS RESOLUTION
Overview
The structure of the heterodimeric flavocytochrome c sulfide dehydrogenase from Chromatium vinosum was determined at a resolution of 2.53 angstroms. It contains a glutathione reductase-like flavin-binding subunit and a diheme cytochrome subunit. The diheme cytochrome folds as two domains, each resembling mitochondrial cytochrome c, and has an unusual interpropionic acid linkage joining the two heme groups in the interior of the subunit. The active site of the flavoprotein subunit contains a catalytically important disulfide bridge located above the pyrimidine portion of the flavin ring. A tryptophan, threonine, or tyrosine side chain may provide a partial conduit for electron transfer to one of the heme groups located 10 angstroms from the flavin.
About this Structure
1FCD is a Protein complex structure of sequences from Allochromatium vinosum with and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium., Chen ZW, Koh M, Van Driessche G, Van Beeumen JJ, Bartsch RG, Meyer TE, Cusanovich MA, Mathews FS, Science. 1994 Oct 21;266(5184):430-2. PMID:7939681
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