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| | ==crystal structure of oxidized hN33/Tusc3== | | ==crystal structure of oxidized hN33/Tusc3== |
| - | <StructureSection load='4m90' size='340' side='right' caption='[[4m90]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='4m90' size='340' side='right'caption='[[4m90]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4m90]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M90 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4m90]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M90 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m8g|4m8g]], [[4m91|4m91]], [[4m92|4m92]]</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]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TUSC3, N33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4m90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m90 OCA], [https://pdbe.org/4m90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m90 RCSB], [https://www.ebi.ac.uk/pdbsum/4m90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m90 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=4m90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m90 OCA], [http://pdbe.org/4m90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m90 RCSB], [http://www.ebi.ac.uk/pdbsum/4m90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m90 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</ref> | + | [https://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</ref> |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Aebi, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Brozzo, M S]] | + | [[Category: Aebi M]] |
| - | [[Category: Glockshuber, R]] | + | [[Category: Brozzo MS]] |
| - | [[Category: Malojcic, G]] | + | [[Category: Glockshuber R]] |
| - | [[Category: Mohorko, E]] | + | [[Category: Malojcic G]] |
| - | [[Category: Owen, R L]] | + | [[Category: Mohorko E]] |
| - | [[Category: Endoplasmic reticulum]]
| + | [[Category: Owen RL]] |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Redox active]]
| + | |
| - | [[Category: Thioredoxin-like fold]]
| + | |
| Structural highlights
Disease
TUSC3_HUMAN Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry.
Function
TUSC3_HUMAN Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.[1]
Publication Abstract from PubMed
N-linked glycosylation of proteins in the endoplasmic reticulum (ER) is essential in eukaryotes and catalyzed by oligosaccharyl transferase (OST). Human OST is a hetero-oligomer of seven subunits. The subunit N33/Tusc3 is a tumor suppressor candidate, and defects in the subunit N33/Tusc3 are linked with nonsyndromic mental retardation. Here, we show that N33/Tusc3 possesses a membrane-anchored N-terminal thioredoxin domain located in the ER lumen that may form transient mixed disulfide complexes with OST substrates. X-ray structures of complexes between N33/Tusc3 and two different peptides as model substrates reveal a defined peptide-binding groove adjacent to the active site that can accommodate peptides in opposite orientations. Structural and biochemical data show that N33/Tusc3 prefers peptides bearing a hydrophobic residue two residues away from the cysteine forming the mixed disulfide with N33/Tusc3. Our results support a model in which N33/Tusc3 increases glycosylation efficiency for a subset of human glycoproteins by slowing glycoprotein folding.
Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation.,Mohorko E, Owen RL, Malojcic G, Brozzo MS, Aebi M, Glockshuber R Structure. 2014 Apr 8;22(4):590-601. doi: 10.1016/j.str.2014.02.013. Epub 2014, Mar 27. PMID:24685145[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhou H, Clapham DE. Mammalian MagT1 and TUSC3 are required for cellular magnesium uptake and vertebrate embryonic development. Proc Natl Acad Sci U S A. 2009 Sep 15;106(37):15750-5. Epub 2009 Aug 26. PMID:19717468 doi:http://dx.doi.org/0908332106
- ↑ Mohorko E, Owen RL, Malojcic G, Brozzo MS, Aebi M, Glockshuber R. Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation. Structure. 2014 Apr 8;22(4):590-601. doi: 10.1016/j.str.2014.02.013. Epub 2014, Mar 27. PMID:24685145 doi:http://dx.doi.org/10.1016/j.str.2014.02.013
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