1syr
From Proteopedia
(Difference between revisions)
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<StructureSection load='1syr' size='340' side='right'caption='[[1syr]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='1syr' size='340' side='right'caption='[[1syr]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1syr]] is a 12 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1syr]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SYR FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1syr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1syr OCA], [https://pdbe.org/1syr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1syr RCSB], [https://www.ebi.ac.uk/pdbsum/1syr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1syr ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Plasmodium falciparum 3D7]] |
| - | [[Category: Hol | + | [[Category: Hol WGJ]] |
| - | [[Category: Robien | + | [[Category: Robien MA]] |
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Current revision
Initial Structural Analysis of Plasmodium falciparum thioredoxin
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