4ysz: Difference between revisions
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==Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with 2-iodo-N-[3-(1-methylethoxy)phenyl]benzamide== | ==Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with 2-iodo-N-[3-(1-methylethoxy)phenyl]benzamide== | ||
<StructureSection load='4ysz' size='340' side='right' caption='[[4ysz]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='4ysz' size='340' side='right'caption='[[4ysz]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ysz]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ysz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YSZ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=12J:2-IODO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE'>12J</scene>, <scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=12J:2-IODO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE'>12J</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=MLI:MALONATE+ION'>MLI</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=4ysz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ysz OCA], [https://pdbe.org/4ysz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ysz RCSB], [https://www.ebi.ac.uk/pdbsum/4ysz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ysz ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/SDHB_ASCSU SDHB_ASCSU] Iron-sulfur protein (Ip) subunit of the mitochondrial electron transport chain complex II which, together with the flavoprotein (Fp) subunit forms the catalytic core of the complex (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436). During the free-living egg-larvae stages, which occur in an aerobic environment, complex II acts as a succinate dehydrogenase by transferring electrons from succinate to ubiquinone (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436). During the parasitic larvae and adult stages, which occur in an anaerobic environment, complex II acts as a fumarate reductase by transferring electrons from rhodoquinol to fumarate (PubMed:10743611, PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7822332, PubMed:8435436).<ref>PMID:10743611</ref> <ref>PMID:12742584</ref> <ref>PMID:17933581</ref> <ref>PMID:2843227</ref> <ref>PMID:7822332</ref> <ref>PMID:8435436</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ysz" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ascaris suum]] | [[Category: Ascaris suum]] | ||
[[Category: Harada | [[Category: Large Structures]] | ||
[[Category: Honma | [[Category: Harada S]] | ||
[[Category: Inaoka | [[Category: Honma T]] | ||
[[Category: Inoue | [[Category: Inaoka DK]] | ||
[[Category: Kita | [[Category: Inoue M]] | ||
[[Category: Nagahama | [[Category: Kita K]] | ||
[[Category: Sakamoto | [[Category: Nagahama M]] | ||
[[Category: Sato | [[Category: Sakamoto K]] | ||
[[Category: Shiba | [[Category: Sato D]] | ||
[[Category: Yamamoto | [[Category: Shiba T]] | ||
[[Category: Yone | [[Category: Yamamoto A]] | ||
[[Category: Yone A]] | |||
