2mmn
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution Structure of the Reduced Thioredoxin from Plasmodium falciparum== | |
| + | <StructureSection load='2mmn' size='340' side='right'caption='[[2mmn]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mmn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MMN FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmn OCA], [https://pdbe.org/2mmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mmn RCSB], [https://www.ebi.ac.uk/pdbsum/2mmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmn ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/THIO1_PLAF7 THIO1_PLAF7] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:11013257, PubMed:20673832). By modifying the redox status of targeted proteins, induces changes in their structure and activity (PubMed:19360125, PubMed:20673832). Reduces oxidized glutathione (GSSG), thereby acting as a backup for the glutathione redox system (PubMed:11013257). Reduces nitroglutathione (GSNO), a compound involved in the transport of nitric oxide (NO) (PubMed:11013257). Also reduces oxidative stress by detoxifying hydrogen peroxide, tert-butyl hydroperoxide and cumene hydroperoxide (PubMed:14962358). Activates ornithine aminotransferase OAT by reducing a disulfide bond in the substrate binding loop, thereby enhancing the affinity of OAT for its substrates (PubMed:20673832). May reduce S-adenosyl-L-homocysteine hydrolase SAHH (PubMed:19360125).<ref>PMID:11013257</ref> <ref>PMID:14962358</ref> <ref>PMID:19360125</ref> <ref>PMID:20673832</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Kalbitzer | + | __TOC__ |
| - | [[Category: Munte | + | </StructureSection> |
| - | [[Category: Schirmer | + | [[Category: Large Structures]] |
| + | [[Category: Plasmodium falciparum 3D7]] | ||
| + | [[Category: Kalbitzer H]] | ||
| + | [[Category: Munte C]] | ||
| + | [[Category: Schirmer R]] | ||
Current revision
Solution Structure of the Reduced Thioredoxin from Plasmodium falciparum
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