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| | ==Crystal structure of Trx3 domain of UGGT (detergent-unbound form)== | | ==Crystal structure of Trx3 domain of UGGT (detergent-unbound form)== |
| - | <StructureSection load='3wzt' size='340' side='right' caption='[[3wzt]], [[Resolution|resolution]] 3.40Å' scene=''> | + | <StructureSection load='3wzt' size='340' side='right'caption='[[3wzt]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wzt]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WZT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WZT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wzt]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WZT FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 3.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wzs|3wzs]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0048990 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</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=3wzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wzt OCA], [https://pdbe.org/3wzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wzt RCSB], [https://www.ebi.ac.uk/pdbsum/3wzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wzt ProSAT]</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=3wzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wzt OCA], [http://pdbe.org/3wzt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wzt RCSB], [http://www.ebi.ac.uk/pdbsum/3wzt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wzt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0SB58_CHATD G0SB58_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| - | [[Category: Kato, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Satoh, T]] | + | [[Category: Kato K]] |
| - | [[Category: Zhu, T]] | + | [[Category: Satoh T]] |
| - | [[Category: Endoplasmic reticulum]] | + | [[Category: Zhu T]] |
| - | [[Category: Folding sensor]]
| + | |
| - | [[Category: Glucosyltransferase]]
| + | |
| - | [[Category: Quality control]]
| + | |
| - | [[Category: Thioredoxin fold]]
| + | |
| - | [[Category: Thioredoxin-like]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
G0SB58_CHATD
Publication Abstract from PubMed
The endoplasmic reticulum (ER) possesses a protein quality control system that supports the efficient folding of newly synthesized glycoproteins. In this system, a series of N-linked glycan intermediates displayed on proteins serve as quality tags. The ER folding-sensor enzyme UDP-glucose:glycoprotein glucosyltransferase (UGGT) operates as the gatekeeper for ER quality control by specifically transferring monoglucose residues to incompletely folded glycoproteins, thereby allowing them to interact with lectin chaperone complexes to facilitate their folding. Despite its functional importance, no structural information is available for this key enzyme to date. To elucidate the folding-sensor mechanism in the ER, we performed a structural study of UGGT. Based on bioinformatics analyses, the folding-sensor region of UGGT was predicted to harbour three tandem thioredoxin (Trx)-like domains, which are often found in proteins involved in ER quality control. Furthermore, we determined the three-dimensional structure of the third Trx-like domain, which exhibits an extensive hydrophobic patch concealed by its flexible C-terminal helix. Our structural data suggest that this hydrophobic patch is involved in intermolecular interactions, thereby contributing to the folding-sensor mechanism of UGGT.
Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase.,Zhu T, Satoh T, Kato K Sci Rep. 2014 Dec 4;4:7322. doi: 10.1038/srep07322. PMID:25471383[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhu T, Satoh T, Kato K. Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase. Sci Rep. 2014 Dec 4;4:7322. doi: 10.1038/srep07322. PMID:25471383 doi:http://dx.doi.org/10.1038/srep07322
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