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| | <StructureSection load='2b5e' size='340' side='right'caption='[[2b5e]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2b5e' size='340' side='right'caption='[[2b5e]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2b5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2b5e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mek|1mek]], [[2bjx|2bjx]], [[2trx|2trx]], [[1eej|1eej]], [[1v57|1v57]], [[1a8y|1a8y]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDI1, MFP1, TRG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></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=2b5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5e OCA], [https://pdbe.org/2b5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5e RCSB], [https://www.ebi.ac.uk/pdbsum/2b5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5e ProSAT]</span></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=2b5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5e OCA], [https://pdbe.org/2b5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5e RCSB], [https://www.ebi.ac.uk/pdbsum/2b5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PDI_YEAST PDI_YEAST]] Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.<ref>PMID:16002399</ref> <ref>PMID:19124653</ref> <ref>PMID:21700223</ref>
| + | [https://www.uniprot.org/uniprot/PDI_YEAST PDI_YEAST] Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.<ref>PMID:16002399</ref> <ref>PMID:19124653</ref> <ref>PMID:21700223</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein disulfide-isomerase]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Schindelin, H]] | + | [[Category: Schindelin H]] |
| - | [[Category: Tian, G]] | + | [[Category: Tian G]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Protein disulfide isomerase]]
| + | |
| Structural highlights
Function
PDI_YEAST Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Protein disulfide isomerase plays a key role in catalyzing the folding of secretory proteins. It features two catalytically inactive thioredoxin domains inserted between two catalytically active thioredoxin domains and an acidic C-terminal tail. The crystal structure of yeast PDI reveals that the four thioredoxin domains are arranged in the shape of a twisted "U" with the active sites facing each other across the long sides of the "U." The inside surface of the "U" is enriched in hydrophobic residues, thereby facilitating interactions with misfolded proteins. The domain arrangement, active site location, and surface features strikingly resemble the Escherichia coli DsbC and DsbG protein disulfide isomerases. Biochemical studies demonstrate that all domains of PDI, including the C-terminal tail, are required for full catalytic activity. The structure defines a framework for rationalizing the differences between the two active sites and their respective roles in catalyzing the formation and rearrangement of disulfide bonds.
The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites.,Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H Cell. 2006 Jan 13;124(1):61-73. PMID:16413482[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kimura T, Hosoda Y, Sato Y, Kitamura Y, Ikeda T, Horibe T, Kikuchi M. Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities. J Biol Chem. 2005 Sep 9;280(36):31438-41. Epub 2005 Jul 7. PMID:16002399 doi:http://dx.doi.org/10.1074/jbc.M503377200
- ↑ Clerc S, Hirsch C, Oggier DM, Deprez P, Jakob C, Sommer T, Aebi M. Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol. 2009 Jan 12;184(1):159-72. doi: 10.1083/jcb.200809198. Epub 2009 Jan, 5. PMID:19124653 doi:http://dx.doi.org/10.1083/jcb.200809198
- ↑ Gauss R, Kanehara K, Carvalho P, Ng DT, Aebi M. A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum. Mol Cell. 2011 Jun 24;42(6):782-93. doi: 10.1016/j.molcel.2011.04.027. PMID:21700223 doi:http://dx.doi.org/10.1016/j.molcel.2011.04.027
- ↑ Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell. 2006 Jan 13;124(1):61-73. PMID:16413482 doi:10.1016/j.cell.2005.10.044
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