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Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition.

Olson LJ, Orsi R, Peterson FC, Parodi AJ, Kim JJ, D'Alessio C, Dahms NM
Biochemistry 54 4097-111 (2015)
Cited: 10 times
EuropePMC logo PMID: 26062005

Abstract

N-Glycans are modified as part of a quality control mechanism during glycoprotein folding in the endoplasmic reticulum (ER). Glucosidase II (GII) plays a critical role by generating monoglucosylated glycans that are recognized by lectin chaperones, calnexin and calreticulin. To understand how the hydrolytic activity of GIIα is enhanced by the mannose 6-phosphate receptor (MPR) homology domain (MRH domain) of its β subunit, we now report a 1.6 Å resolution crystal structure of the MRH domain of GIIβ bound to mannose. A comparison of ligand-bound and unbound structures reveals no major difference in their overall fold, but rather a repositioning of side chains throughout the binding pocket, including Y372. Mutation of Y372 inhibits GII activity, demonstrating an important role for Y372 in regulating GII activity. Comparison of the MRH domains of GIIβ, MPRs, and the ER lectin OS-9 identified conserved residues that are critical for the structural integrity and architecture of the carbohydrate binding pocket. As shown by nuclear magnetic resonance spectroscopy, mutations of the primary binding pocket residues and adjacent W409, all of which inhibit the activity of GII both in vitro and in vivo, do not cause a significant change in the overall fold of the GIIβ MRH domain but impact locally the stability of the binding pocket. W409 does not directly contact mannose; rather, its indole ring is stabilized by binding into a hydrophobic pocket of an adjacent crystallographic neighbor. This suggests that W409 interacts with a hydrophobic region of the GIIβ or GIIα subunit to modulate its effect on GII activity.

Reviews - 4xqm mentioned but not cited (1)

  1. Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi. Barre A, Bourne Y, Van Damme EJM, Rougé P. Int J Mol Sci 20 E254 (2019)

Articles - 4xqm mentioned but not cited (2)

  1. Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition. Olson LJ, Orsi R, Peterson FC, Parodi AJ, Kim JJ, D'Alessio C, Dahms NM. Biochemistry 54 4097-4111 (2015)
  2. Structures of the mannose-6-phosphate pathway enzyme, GlcNAc-1-phosphotransferase. Gorelik A, Illes K, Bui KH, Nagar B. Proc Natl Acad Sci U S A 119 e2203518119 (2022)


Reviews citing this publication (1)

  1. A sweet code for glycoprotein folding. Caramelo JJ, Parodi AJ. FEBS Lett 589 3379-3387 (2015)

Articles citing this publication (6)

  1. Structures of mammalian ER α-glucosidase II capture the binding modes of broad-spectrum iminosugar antivirals. Caputo AT, Alonzi DS, Marti L, Reca IB, Kiappes JL, Struwe WB, Cross A, Basu S, Lowe ED, Darlot B, Santino A, Roversi P, Zitzmann N. Proc Natl Acad Sci U S A 113 E4630-8 (2016)
  2. Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control. Satoh T, Toshimori T, Yan G, Yamaguchi T, Kato K. Sci Rep 6 20575 (2016)
  3. Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control. Satoh T, Toshimori T, Noda M, Uchiyama S, Kato K. Protein Sci 25 2095-2101 (2016)
  4. Substrate recognition of the catalytic α-subunit of glucosidase II from Schizosaccharomyces pombe. Okuyama M, Miyamoto M, Matsuo I, Iwamoto S, Serizawa R, Tanuma M, Ma M, Klahan P, Kumagai Y, Tagami T, Kimura A. Biosci Biotechnol Biochem 81 1503-1511 (2017)
  5. A Peptide-Lectin Fusion Strategy for Developing a Glycan Probe for Use in Various Assay Formats. Lim B, Kydd L, Jaworski J. Chemosensors (Basel) 7 55 (2019)
  6. Proteome and transcriptome analyses of wheat near isogenic lines identifies key proteins and genes of wheat bread quality. Lv L, Zhao A, Zhang Y, Li H, Chen X. Sci Rep 11 9978 (2021)


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