Flavocytochrome: Difference between revisions

Jump to navigation Jump to search
Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
 
(34 intermediate revisions by 3 users not shown)
Line 1: Line 1:
{{STRUCTURE_1kbi|  PDB=1kbi  | SIZE=400| SCENE=Flavocytochrome/Cv/1 |right|CAPTION=Yeast flavocytochrome b2 flavin-binding domain dimer complex with FMN, MPD, phosphate, pyruvic acid [[1kbi]] }}
<StructureSection load='2b7r' size='450' side='right' caption='Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid (PDB code [[2b7r]]).' scene='' >


* '''Flavocytochrome b2''' (Fcb2) is a flavin-dependent hydroxy acid dehydrogenase.<br />
*  '''FP450 BM3''' is a fatty acid hydroxtylase from ''Bacillus'' ''megaterium''.<br />
*  '''Fcc''' catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.<br />
*  '''Fcc3''' has fumarate reductase activity.


== 3D Structures of flavocytochrome ==
* '''Flavocytochrome c''' or '''flavocytochrome c sulphide dehydrogenase''' or  '''Fcc''' catalyzes the conversion of H2S and ferricytochrome c to S and ferrocytochrome c.<br />
*  '''Fcc3''' has fumarate reductase activity<ref>PMID:12093271</ref> 
* '''Flavocytochrome b2''' is a L-lactate/cytochrome c oxidoreductase<ref>PMID:15260495</ref>
* '''Flavocytochrome b558''' is the catalytic component of the phagocyte NADPH oxidase
 
<scene name='44/442751/Cv/10'>Structure of heme-containing flavocytochrome c3 complex with FAD and fumaric acid</scene> (PDB code [[2b7r]]<ref>PMID:16699170</ref>).
*<scene name='44/442751/Cv/12'>1st Heme binding site</scene>. Water molecules are shown as red spheres.
*<scene name='44/442751/Cv/13'>1st Heme Fe coordination site</scene>.
*<scene name='44/442751/Cv/14'>2nd Heme binding site</scene>.
*<scene name='44/442751/Cv/15'>2nd Heme Fe coordination site</scene>.
*<scene name='44/442751/Cv/16'>3rd Heme binding site</scene>.
*<scene name='44/442751/Cv/17'>3rd Heme Fe coordination site</scene>.
*<scene name='44/442751/Cv/18'>4th Heme binding site</scene>.
*<scene name='44/442751/Cv/19'>4th Heme Fe coordination site</scene>.


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Interestedly, that all 4 heme groups are <scene name='44/442751/Cv/20'>covalently bound with Cys residues</scene> in heme-containing flavocytochrome c3 (PDB code [[2b7r]]).


===FP450===
<scene name='44/442751/Cv/26'>All Fe of 4 heme groups are coordinated with His residues</scene>.


[[3kx3]], [[3kx4]], [[3kx5]], [[3ekb]], [[3ekd]], [[3ekf]], [[3nnb]], [[2yqo]], [[2yqp]], [[1p0v]], [[1p0w]], [[1p0x]], [[1jme]] – BmFP450 BM3 (mutant) – ''Bacillus megaterium''<br />
<scene name='44/442751/Cv/22'>Fumaric acid binding site</scene>.
[[2ij2]] - BmFP450 BM3<br />
[[2uwh]] - BmFP450 BM3 (mutant)+palmitic acid<br />
[[2j1m]], [[2j4s]] - BmFP450 BM3 + DMSO<br />
[[3ben]] - BmFP450 BM3 heme domain+inhibitor<br />
[[3vrd]] – Fc heme and FMN binding domains – ''Thermochromatium tepidum''


===Fcb2===
<scene name='44/442751/Cv/24'>FAD binding site</scene>.


[[3ks0]] – mFcb2 heme domain+fragment antigen binding B2B4+Cyt b2 – mouse<br />
<scene name='44/442751/Cv/25'>Na coordination site</scene>.
[[2oz0]], [[1qcw]] – yFcb2 (mutant) – yeast<br />
[[1kbi]], [[1fcb]] – yFcb2<br />
[[1kbj]] – yFcb2 FMN binding domain<br />
[[1sze]] – yFcb2 (mutant)+benzoylformate<br />
[[1szf]], [[1lco]], [[1ldc]] – yFcb2 (mutant)+pyruvate derivative<br />
[[1szg]] – yFcb2 (mutant)+sulfite<br />
[[1ltd]] – yFcb2 +sulfite


===Fcc===
== 3D Structures of flavocytochrome ==
[[Flavocytochrome 3D structures]]


[[2b7r]], [[2b7s]], [[1q9i]], [[1p2e]], [[1p2h]], [[1lj1]], [[1m64]], [[1kss]], [[1ksu]], [[1jrx]], [[1jry]], [[1jrz]], [[1e39]] – SfFcc3 (mutant) – ''Shewanella frigidimarina''<br />
</StructureSection>
[[1qo8]], [[1qjd]] - SfFcc3<br />
[[1y0p]] – SfFcc3+mesaconate<br />
[[1wve]] – Fcc+4-cresol dehydrogenase – ''Pseudomonas putida''


[[1wlp]] – Fc B-245 light chain - human
== References ==
<references/>


[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman