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1nen
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1nen" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nen, resolution 2.9Å" /> '''Complex II (Succinate...) |
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| - | [[Image:1nen.jpg|left|200px]]<br /><applet load="1nen" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1nen, resolution 2.9Å" /> | ||
| - | '''Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site'''<br /> | ||
| - | == | + | ==Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site== |
| - | + | <StructureSection load='1nen' size='340' side='right'caption='[[1nen]], [[Resolution|resolution]] 2.90Å' scene=''> | |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1nen]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NEN 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]] 2.9Å</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=DNT:2-[1-METHYLHEXYL]-4,6-DINITROPHENOL'>DNT</scene>, <scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</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=SF4:IRON/SULFUR+CLUSTER'>SF4</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=1nen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nen OCA], [https://pdbe.org/1nen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nen RCSB], [https://www.ebi.ac.uk/pdbsum/1nen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nen 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/1nen_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1nen ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]] | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Byrne | + | [[Category: Byrne B]] |
| - | [[Category: Cecchini | + | [[Category: Cecchini G]] |
| - | [[Category: Horsefield | + | [[Category: Horsefield R]] |
| - | [[Category: Iwata | + | [[Category: Iwata S]] |
| - | [[Category: Leger | + | [[Category: Leger C]] |
| - | [[Category: Luna-Chavez | + | [[Category: Luna-Chavez C]] |
| - | [[Category: Miyoshi | + | [[Category: Miyoshi H]] |
| - | [[Category: Tornroth | + | [[Category: Tornroth S]] |
| - | [[Category: Yankovskaya | + | [[Category: Yankovskaya V]] |
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Current revision
Complex II (Succinate Dehydrogenase) From E. Coli with Dinitrophenol-17 inhibitor co-crystallized at the ubiquinone binding site
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