2K46
Xenopus laevis malectin complexed with nigerose (Glcalpha1-3Glc)
Summary for 2K46
| Entry DOI | 10.2210/pdb2k46/pdb |
| Related | 2jwp |
| Related PRD ID | PRD_900052 |
| Descriptor | MGC80075 protein, alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose (2 entities in total) |
| Functional Keywords | carbohydrate recognition domain, glc2-high-mannose-n-glycan, nigerose, sugar binding protein |
| Biological source | Xenopus laevis (African clawed frog) |
| Cellular location | Endoplasmic reticulum membrane; Single-pass type I membrane protein: Q6INX3 |
| Total number of polymer chains | 1 |
| Total formula weight | 21542.30 |
| Authors | Schallus, T. (deposition date: 2008-05-28, release date: 2008-08-12, Last modification date: 2024-05-01) |
| Primary citation | Schallus, T.,Jaeckh, C.,Feher, K.,Palma, A.S.,Liu, Y.,Simpson, J.C.,Mackeen, M.,Stier, G.,Gibson, T.J.,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.Cell.Biol., 19:3404-3414, 2008 Cited by PubMed Abstract: 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. PubMed: 18524852DOI: 10.1091/mbc.E08-04-0354 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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