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4m90

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Revision as of 07:42, 11 August 2016

crystal structure of oxidized hN33/Tusc3

Structural highlights

4m90 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4m8g, 4m91, 4m92
Gene:	TUSC3, N33 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4m90"

@@ Line 1: / Line 1: @@
 ==crystal structure of oxidized hN33/Tusc3==
 <StructureSection load='4m90' size='340' side='right' caption='[[4m90]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </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>
 <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'>[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://www.rcsb.org/pdb/explore.do?structureId=4m90 RCSB], [http://www.ebi.ac.uk/pdbsum/4m90 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=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>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4m90" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4m90

From Proteopedia

Revision as of 07:42, 11 August 2016

crystal structure of oxidized hN33/Tusc3

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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