4tve: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure Of the First Two Thioredoxin Domains of Naumovozyma dairenensis Eps1p== | ==Structure Of the First Two Thioredoxin Domains of Naumovozyma dairenensis Eps1p== | ||
<StructureSection load='4tve' size='340' side='right' caption='[[4tve]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4tve' size='340' side='right' caption='[[4tve]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| Line 5: | Line 6: | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tw5|4tw5]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tw5|4tw5]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.1 5.4.3.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deleted_entry Deleted entry], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.1 5.4.3.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tve OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tve RCSB], [http://www.ebi.ac.uk/pdbsum/4tve PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tve OCA], [http://pdbe.org/4tve PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tve RCSB], [http://www.ebi.ac.uk/pdbsum/4tve PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tve ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 15: | Line 16: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4tve" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 25: | ||
[[Category: Deborah, F]] | [[Category: Deborah, F]] | ||
[[Category: Endoplasmic reticulum]] | [[Category: Endoplasmic reticulum]] | ||
[[Category: Isomerase]] | |||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Protein disulfide isomerase]] | [[Category: Protein disulfide isomerase]] | ||
[[Category: Thioredoxin]] | [[Category: Thioredoxin]] | ||
Revision as of 11:05, 27 July 2016
Structure Of the First Two Thioredoxin Domains of Naumovozyma dairenensis Eps1pStructure Of the First Two Thioredoxin Domains of Naumovozyma dairenensis Eps1p
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||