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==Xenopus laevis malectin complexed with nigerose (Glcalpha1-3Glc)==
==Xenopus laevis malectin complexed with nigerose (Glcalpha1-3Glc)==
<StructureSection load='2k46' size='340' side='right'caption='[[2k46]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2k46' size='340' side='right'caption='[[2k46]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2k46]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K46 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2k46]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K46 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jwp|2jwp]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900052:alpha-nigerose'>PRD_900052</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MGC80075 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis])</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=2k46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k46 OCA], [https://pdbe.org/2k46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k46 RCSB], [https://www.ebi.ac.uk/pdbsum/2k46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k46 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=2k46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k46 OCA], [https://pdbe.org/2k46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k46 RCSB], [https://www.ebi.ac.uk/pdbsum/2k46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k46 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MLECA_XENLA MLECA_XENLA]] Carbohydate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation. Can bind di- or higher oligomers but not monomers of glucose, including maltose, maltotriose, maltotetraose, maltoheptaose, nigerose, kojibose, cellobiose and isomaltose, although based on their subcellular locations, these are unlikely to all be physiological ligands.<ref>PMID:18524852</ref>
[https://www.uniprot.org/uniprot/MLECA_XENLA MLECA_XENLA] Carbohydate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation. Can bind di- or higher oligomers but not monomers of glucose, including maltose, maltotriose, maltotetraose, maltoheptaose, nigerose, kojibose, cellobiose and isomaltose, although based on their subcellular locations, these are unlikely to all be physiological ligands.<ref>PMID:18524852</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k46 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2k46 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
N-Glycosylation starts in the endoplasmic reticulum (ER) where a 14-sugar glycan composed of three glucoses, nine mannoses, and two N-acetylglucosamines (Glc(3)Man(9)GlcNAc(2)) is transferred to nascent proteins. The glucoses are sequentially trimmed by ER-resident glucosidases. The Glc(3)Man(9)GlcNAc(2) moiety is the substrate for oligosaccharyltransferase; the Glc(1)Man(9)GlcNAc(2) and Man(9)GlcNAc(2) intermediates are signals for glycoprotein folding and quality control in the calnexin/calreticulin cycle. Here, we report a novel membrane-anchored ER protein that is highly conserved in animals and that recognizes the Glc(2)-N-glycan. Structure determination by nuclear magnetic resonance showed that its luminal part is a carbohydrate binding domain that recognizes glucose oligomers. Carbohydrate microarray analyses revealed a uniquely selective binding to a Glc(2)-N-glycan probe. The localization, structure, and binding specificity of this protein, which we have named malectin, open the way to studies of its role in the genesis, processing and secretion of N-glycosylated proteins.
Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation.,Schallus T, Jaeckh C, Feher K, Palma AS, Liu Y, Simpson JC, Mackeen M, Stier G, Gibson TJ, Feizi T, Pieler T, Muhle-Goll C Mol Biol Cell. 2008 Aug;19(8):3404-14. Epub 2008 Jun 4. PMID:18524852<ref>PMID:18524852</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2k46" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Schallus, T]]
[[Category: Schallus T]]
[[Category: Carbohydrate recognition domain]]
[[Category: Glc2-high-mannose-n-glycan]]
[[Category: Nigerose]]
[[Category: Sugar binding protein]]

Latest revision as of 09:44, 1 May 2024

Xenopus laevis malectin complexed with nigerose (Glcalpha1-3Glc)Xenopus laevis malectin complexed with nigerose (Glcalpha1-3Glc)

Structural highlights

2k46 is a 1 chain structure with sequence from Xenopus laevis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MLECA_XENLA Carbohydate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation. Can bind di- or higher oligomers but not monomers of glucose, including maltose, maltotriose, maltotetraose, maltoheptaose, nigerose, kojibose, cellobiose and isomaltose, although based on their subcellular locations, these are unlikely to all be physiological ligands.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Schallus T, Jaeckh C, Feher K, Palma AS, Liu Y, Simpson JC, Mackeen M, Stier G, Gibson TJ, Feizi T, Pieler T, Muhle-Goll C. Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Mol Biol Cell. 2008 Aug;19(8):3404-14. Epub 2008 Jun 4. PMID:18524852 doi:10.1091/mbc.E08-04-0354
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