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TitleStructure of the murine lysosomal multienzyme complex core.
Journal, issue, pagesSci Adv, Vol. 7, Issue 20, Year 2021
Publish dateMay 12, 2021
AuthorsAlexei Gorelik / Katalin Illes / S M Naimul Hasan / Bhushan Nagar / Mohammad T Mazhab-Jafari /
PubMed AbstractThe enzymes β-galactosidase (GLB1) and neuraminidase 1 (NEU1; sialidase 1) participate in the degradation of glycoproteins and glycolipids in the lysosome. To remain active and stable, they ...The enzymes β-galactosidase (GLB1) and neuraminidase 1 (NEU1; sialidase 1) participate in the degradation of glycoproteins and glycolipids in the lysosome. To remain active and stable, they associate with PPCA [protective protein cathepsin A (CTSA)] into a high-molecular weight lysosomal multienzyme complex (LMC), of which several forms exist. Genetic defects in these three proteins cause the lysosomal storage diseases GM1-gangliosidosis/mucopolysaccharidosis IV type B, sialidosis, and galactosialidosis, respectively. To better understand the interactions between these enzymes, we determined the three-dimensional structure of the murine LMC core. This 0.8-MDa complex is composed of three GLB1 dimers and three CTSA dimers, adopting a triangular architecture maintained through six copies of a unique GLB1-CTSA polar interface. Mutations in this contact surface that occur in GM1-gangliosidosis prevent formation of the LMC in vitro. These findings may facilitate development of therapies for lysosomal storage disorders.
External linksSci Adv / PubMed:33980489 / PubMed Central
MethodsEM (single particle)
Resolution4.59 Å
Structure data

22830

7kdv

EMDB-22830, PDB-7kdv:
Murine core lysosomal multienzyme complex (LMC) composed of acid beta-galactosidase (GLB1) and protective protein cathepsin A (PPCA, CTSA)
Method: EM (single particle) / Resolution: 4.59 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • mus musculus (house mouse)
KeywordsHYDROLASE / glycosidase / protease / lysosome

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