1nek: Difference between revisions
New page: left|200px<br /><applet load="1nek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nek, resolution 2.60Å" /> '''Complex II (Succinat... |
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[[Image:1nek.gif|left|200px]]<br /><applet load="1nek" size=" | [[Image:1nek.gif|left|200px]]<br /><applet load="1nek" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nek, resolution 2.60Å" /> | caption="1nek, resolution 2.60Å" /> | ||
'''Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound'''<br /> | '''Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of Escherichia coli succinate dehydrogenase (SQR), analogous | 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. | ||
==About this Structure== | ==About this Structure== | ||
1NEK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with OAA, CA, FAD, FES, SF4, F3S, HEM, UQ2, CDN and EPH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1NEK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=OAA:'>OAA</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=FES:'>FES</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=F3S:'>F3S</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=UQ2:'>UQ2</scene>, <scene name='pdbligand=CDN:'>CDN</scene> and <scene name='pdbligand=EPH:'>EPH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEK OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: oxygen respiratory chain]] | [[Category: oxygen respiratory chain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:14 2008'' | ||
Revision as of 15:05, 21 February 2008
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Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound
OverviewOverview
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.
About this StructureAbout this Structure
1NEK is a Protein complex structure of sequences from Escherichia coli with , , , , , , , , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Feb 21 14:05:14 2008