1nek
From Proteopedia
| Line 1: | Line 1: | ||
| - | {{Seed}} | ||
[[Image:1nek.png|left|200px]] | [[Image:1nek.png|left|200px]] | ||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_1nek", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_1nek| PDB=1nek | SCENE= }} | {{STRUCTURE_1nek| PDB=1nek | SCENE= }} | ||
===Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound=== | ===Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound=== | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, {{ABSTRACT_PUBMED_12560550}}, adds the Publication Abstract to the page | ||
| - | (as it appears on PubMed at http://www.pubmed.gov), where 12560550 is the PubMed ID number. | ||
| - | --> | ||
{{ABSTRACT_PUBMED_12560550}} | {{ABSTRACT_PUBMED_12560550}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1nek]] is a 4 chain structure of [[Succinate Dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEK OCA]. | |
| + | |||
| + | ==See Also== | ||
| + | *[[Succinate Dehydrogenase|Succinate Dehydrogenase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:012560550</ref><ref group="xtra">PMID:015109257</ref><references group="xtra"/> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Byrne, B.]] | [[Category: Byrne, B.]] | ||
| Line 35: | Line 26: | ||
[[Category: Yankovskaya, V.]] | [[Category: Yankovskaya, V.]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
| - | [[Category: Oxidoreductase | + | [[Category: Oxidoreductase-electron transport complex]] |
[[Category: Oxygen respiratory chain]] | [[Category: Oxygen respiratory chain]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 2 16:17:24 2009'' | ||
Revision as of 06:31, 27 July 2012
| |||||||||
| 1nek, resolution 2.60Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , , , , | ||||||||
| Gene: | SDHA OR B0723 OR Z0877 OR ECS0748 (Escherichia coli), SDHB OR B0724 (Escherichia coli), SDHC OR CYBA OR B0721 OR Z0875 OR ECS0746 (Escherichia coli), SDHD OR B0722 (Escherichia coli) | ||||||||
| Related: | 1nen | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound
The structure of Escherichia coli succinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron donor, succinate, to the terminal electron acceptor, ubiquinone. It was found that the SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species (ROS) formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of ROS. Furthermore, symptoms of genetic disorders associated with mitochondrial SQR mutations may be a result of ROS formation resulting from impaired electron transport in the enzyme.
Architecture of succinate dehydrogenase and reactive oxygen species generation., Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S, Science. 2003 Jan 31;299(5607):700-4. PMID:12560550
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1nek is a 4 chain structure of Succinate Dehydrogenase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 2003 Jan 31;299(5607):700-4. PMID:12560550 doi:10.1126/science.1079605
- Rothery EL, Mowat CG, Miles CS, Mott S, Walkinshaw MD, Reid GA, Chapman SK. Probing domain mobility in a flavocytochrome. Biochemistry. 2004 May 4;43(17):4983-9. PMID:15109257 doi:10.1021/bi030261w
