View source for 5zpv


==Solution Structure of Thioredoxin-Like Effector Protein (TRX3) from Edwardsiella piscicida==
<StructureSection load='5zpv' size='340' side='right'caption='[[5zpv]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zpv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Edwardsiella_tarda_EIB202 Edwardsiella tarda EIB202]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZPV 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=5zpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zpv OCA], [https://pdbe.org/5zpv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zpv RCSB], [https://www.ebi.ac.uk/pdbsum/5zpv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zpv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D0Z9P5_EDWTE D0Z9P5_EDWTE] 
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== Publication Abstract from PubMed ==
Redox signaling and homeostasis are essential for cell survival and the immune response. Peroxiredoxin (Prx) modulates the level of H2O2 as a redox signal through H2O2 decomposition. The redox activity of thioredoxin (Trx) is required as a reducing equivalent to regenerate Prx. Edwardsiella piscicida is an opportunistic Gram-negative enteric pathogen that secretes a novel Trx-like effector protein, ETAE_2186 (Trxlp). Trxlp has unique structural properties compared with other Trx proteins. In enzymatic and binding assays, we confirmed Trxlp to be redox-inactive due to the low reactivity and flexibility of the resolving cysteine residue, C35, at the active site motif "(31)WCXXC(35)". We identified key residues near the active site that are critical for reactivity and flexibility of C35 by site-directed mutagenesis analysis. NMR titration experiment demonstrated prolong inhibitory interaction of Trxlp with Prx1 resulting in the repression of Prx1-mediated H2O2 decomposition leading to increased ROS accumulation in infected host cells. Increased ROS in turn prevented nuclear translocation of NF-kappaB and inhibition of NF-kappaB target genes, leading to bacterial survival and enhanced replication inside host cells. Targeting Trxlp-mediated virulence promises to attenuate E. piscicida infection.

Trxlp, a thioredoxin-like effector from Edwardsiella piscicida inhibits cellular redox signaling and nuclear translocation of NF-kappaB.,Sayed A, Chakraborty S, Leung KY, Sugii S, Mok YK Int J Biol Macromol. 2020 Apr 1;148:89-101. doi: 10.1016/j.ijbiomac.2020.01.114. , Epub 2020 Jan 13. PMID:31945434<ref>PMID:31945434</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5zpv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Edwardsiella tarda EIB202]]
[[Category: Large Structures]]
[[Category: Mok YK]]
[[Category: Sayed AM]]