1d4d: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: left|200px<br /><applet load="1d4d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d4d, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1d4d.jpg|left|200px]]<br /><applet load="1d4d" size=" | [[Image:1d4d.jpg|left|200px]]<br /><applet load="1d4d" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1d4d, resolution 2.5Å" /> | caption="1d4d, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF THE SUCCINATE COMPLEXED FORM OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1'''<br /> | '''CRYSTAL STRUCTURE OF THE SUCCINATE COMPLEXED FORM OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1'''<br /> | ||
==Overview== | ==Overview== | ||
Fumarate respiration is one of the most widespread types of anaerobic | Fumarate respiration is one of the most widespread types of anaerobic respiration. The soluble fumarate reductase of Shewanella putrefaciens MR-1 is a periplasmic tetraheme flavocytochrome c. The crystal structures of the enzyme were solved to 2.9 A for the uncomplexed form and to 2.8 A and 2.5 A for the fumarate and the succinate-bound protein, respectively. The structures reveal a flexible capping domain linked to the FAD-binding domain. A catalytic mechanism for fumarate reduction based on the structure of the complexed protein is proposed. The mechanism for the reverse reaction is a model for the homologous succinate dehydrogenase (complex II) of the respiratory chain. In flavocytochrome c fumarate reductase, all redox centers are in van der Waals contact with one another, thus providing an efficient conduit of electrons from the hemes via the FAD to fumarate. | ||
==About this Structure== | ==About this Structure== | ||
1D4D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens] with HEM, FAD and SIN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] Full crystallographic information is available from [http:// | 1D4D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens] with <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=SIN:'>SIN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4D OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Succinate dehydrogenase]] | [[Category: Succinate dehydrogenase]] | ||
[[Category: Beeumen, J | [[Category: Beeumen, J J.Van.]] | ||
[[Category: Cusanovich, M | [[Category: Cusanovich, M A.]] | ||
[[Category: Leys, D.]] | [[Category: Leys, D.]] | ||
[[Category: Meyer, T | [[Category: Meyer, T E.]] | ||
[[Category: Tsapin, A | [[Category: Tsapin, A S.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
| Line 24: | Line 24: | ||
[[Category: tetraheme flavocytochrome c fumarate reductase]] | [[Category: tetraheme flavocytochrome c fumarate reductase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:55 2008'' | ||