2n1h: Difference between revisions

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New page: '''Unreleased structure''' The entry 2n1h is ON HOLD Authors: Olson, L.J., Peterson, F.C., Damhs, N.M. Description: Solution structure of the GBII-beta MRH domain W409A point mutant [[...
 
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'''Unreleased structure'''


The entry 2n1h is ON HOLD
==Solution structure of the GBII-beta MRH domain W409A point mutant==
<StructureSection load='2n1h' size='340' side='right'caption='[[2n1h]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2n1h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1H FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2n1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1h OCA], [https://pdbe.org/2n1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1h RCSB], [https://www.ebi.ac.uk/pdbsum/2n1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLU2B_SCHPO GLU2B_SCHPO] Subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins in the endoplasmic reticulum (ER). Specifically required for the cleavage of the final glucose. The subunit beta retains the catalytic subunit alpha in the ER.<ref>PMID:10464333</ref> <ref>PMID:19605557</ref> <ref>PMID:21471007</ref>


Authors: Olson, L.J., Peterson, F.C., Damhs, N.M.
==See Also==
 
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
Description: Solution structure of the GBII-beta MRH domain W409A point mutant
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Damhs, N.M]]
__TOC__
[[Category: Olson, L.J]]
</StructureSection>
[[Category: Peterson, F.C]]
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe 972h-]]
[[Category: Damhs NM]]
[[Category: Olson LJ]]
[[Category: Peterson FC]]

Latest revision as of 04:12, 21 November 2024

Solution structure of the GBII-beta MRH domain W409A point mutantSolution structure of the GBII-beta MRH domain W409A point mutant

Structural highlights

2n1h is a 1 chain structure with sequence from Schizosaccharomyces pombe 972h-. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 20 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLU2B_SCHPO Subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins in the endoplasmic reticulum (ER). Specifically required for the cleavage of the final glucose. The subunit beta retains the catalytic subunit alpha in the ER.[1] [2] [3]

See Also

References

  1. D'Alessio C, Fernandez F, Trombetta ES, Parodi AJ. Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding. J Biol Chem. 1999 Sep 3;274(36):25899-905. PMID:10464333
  2. Stigliano ID, Caramelo JJ, Labriola CA, Parodi AJ, D'Alessio C. Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals. Mol Biol Cell. 2009 Sep;20(17):3974-84. Epub 2009 Jul 15. PMID:19605557 doi:E09-04-0316
  3. Stigliano ID, Alculumbre SG, Labriola CA, Parodi AJ, D'Alessio C. Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo. Mol Biol Cell. 2011 Jun 1;22(11):1810-23. doi: 10.1091/mbc.E11-01-0019. Epub 2011, Apr 6. PMID:21471007 doi:10.1091/mbc.E11-01-0019
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