2mmo: Difference between revisions

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'''Unreleased structure'''


The entry 2mmo is ON HOLD
==Solution Structure of the oxidised Thioredoxin from Plasmodium falciparum==
<StructureSection load='2mmo' size='340' side='right'caption='[[2mmo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mmo]] 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=2MMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MMO FirstGlance]. <br>
</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=2mmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mmo OCA], [https://pdbe.org/2mmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mmo RCSB], [https://www.ebi.ac.uk/pdbsum/2mmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mmo 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>


Authors: Munte, C., Kalbitzer, H., Schirmer, R.
==See Also==
 
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
Description: Solution Structure of the oxidised Thioredoxin from Plasmodium falciparum
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum 3D7]]
[[Category: Kalbitzer H]]
[[Category: Munte C]]
[[Category: Schirmer R]]