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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== | ==Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound== | ||
The structure of Escherichia coli succinate dehydrogenase (SQR), analogous | <StructureSection load='1nek' size='340' side='right'caption='[[1nek]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1nek]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The October 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Citric Acid Cycle'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_10 10.2210/rcsb_pdb/mom_2012_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CDN:CARDIOLIPIN'>CDN</scene>, <scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OAA:OXALOACETATE+ION'>OAA</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nek OCA], [https://pdbe.org/1nek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nek RCSB], [https://www.ebi.ac.uk/pdbsum/1nek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nek ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SDHA_ECOLI SDHA_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.<ref>PMID:24374335</ref> <ref>PMID:12560550</ref> <ref>PMID:16407191</ref> <ref>PMID:19710024</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/1nek_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nek ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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<ref>PMID:12560550</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1nek" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Succinate Dehydrogenase|Succinate Dehydrogenase]] | |||
*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Citric Acid Cycle]] | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Byrne | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Cecchini | [[Category: Byrne B]] | ||
[[Category: Horsefield | [[Category: Cecchini G]] | ||
[[Category: Iwata | [[Category: Horsefield R]] | ||
[[Category: Leger | [[Category: Iwata S]] | ||
[[Category: Luna-Chavez | [[Category: Leger C]] | ||
[[Category: Miyoshi | [[Category: Luna-Chavez C]] | ||
[[Category: Tornroth | [[Category: Miyoshi H]] | ||
[[Category: Yankovskaya | [[Category: Tornroth S]] | ||
[[Category: Yankovskaya V]] | |||
