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Structural investigation of glycan recognition by the ERAD quality control lectin Yos9

Item Type:Article
Title:Structural investigation of glycan recognition by the ERAD quality control lectin Yos9
Creators Name:Kniss, A. and Kazemi, S. and Löhr, F. and Berger, M. and Rogov, V.V. and Güntert, P. and Sommer, T. and Jarosch, E. and Dötsch, V.
Abstract:Yos9 is an essential component of the endoplasmic reticulum associated protein degradation (ERAD) system that is responsible for removing terminally misfolded proteins from the ER lumen and mediating proteasomal degradation in the cytosol. Glycoproteins that fail to attain their native conformation in the ER expose a distinct oligosaccharide structure, a terminal α1,6-linked mannose residue, that is specifically recognized by the mannose 6-phoshate receptor homology (MRH) domain of Yos9. We have determined the structure of the MRH domain of Yos9 in its free form and complexed with 3α, 6α-mannopentaose. We show that binding is achieved by loops between β-strands performing an inward movement and that this movement also affects the entire β-barrel leading to a twist. These rearrangements may facilitate the processing of client proteins by downstream acting factors. In contrast, other oligosaccharides such as 2α-mannobiose bind weakly with only locally occurring chemical shift changes underscoring the specificity of this substrate selection process within ERAD.
Keywords:Endoplasmatic Reticulum Associated Protein Degradation, Yos9, Glycan Binding, Conformational Change
Source:Journal of Biomolecular NMR
ISSN:0925-2738
Publisher:Springer (The Netherlands)
Volume:72
Number:1-2
Page Range:1-10
Date:October 2018
Official Publication:https://doi.org/10.1007/s10858-018-0201-6
PubMed:View item in PubMed

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