View source for 4tve


==Structure Of the First Two Thioredoxin Domains of Naumovozyma dairenensis Eps1p==
<StructureSection load='4tve' size='340' side='right'caption='[[4tve]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4tve]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naumovozyma_dairenensis_CBS_421 Naumovozyma dairenensis CBS 421]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TVE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TVE 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=4tve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tve OCA], [https://pdbe.org/4tve PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tve RCSB], [https://www.ebi.ac.uk/pdbsum/4tve PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tve ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0W5T0_NAUDC G0W5T0_NAUDC] 
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== Publication Abstract from PubMed ==
The widespread thioredoxin superfamily enzymes typically share the following features: a characteristic alpha-beta fold, the presence of a Cys-X-X-Cys (or Cys-X-X-Ser) redox-active motif, and a proline in the cis configuration abutting the redox-active site in the tertiary structure. The Cys-X-X-Cys motif is at the solvent-exposed amino terminus of an alpha-helix, allowing the first cysteine to engage in nucleophilic attack on substrates, or substrates to attack the Cys-X-X-Cys disulfide, depending on whether the enzyme functions to reduce, isomerize, or oxidize its targets. We report here the X-ray crystal structure of an enzyme that breaks many of our assumptions regarding the sequence-structure relationship of thioredoxin superfamily proteins. The yeast Protein Disulfide Isomerase family member Eps1p has Cys-X-X-Cys motifs and proline residues at the appropriate primary structural positions in its first two predicted thioredoxin-fold domains. However, crystal structures show that the Cys-X-X-Cys of the second domain is buried and that the adjacent proline is in the trans, rather than the cis isomer. In these configurations, neither the "active-site" disulfide nor the backbone carbonyl preceding the proline is available to interact with substrate. The Eps1p structures thus expand the documented diversity of the PDI oxidoreductase family and demonstrate that conserved sequence motifs in common folds do not guarantee structural or functional conservation.

The eps1p protein disulfide isomerase conserves classic thioredoxin superfamily amino Acid motifs but not their functional geometries.,Biran S, Gat Y, Fass D PLoS One. 2014 Dec 1;9(12):e113431. doi: 10.1371/journal.pone.0113431., eCollection 2014. PMID:25437863<ref>PMID:25437863</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 4tve" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Naumovozyma dairenensis CBS 421]]
[[Category: Biran S]]
[[Category: Deborah F]]