ArticleFEBS open bio2020
Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.
Article in FEBS open bio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Mechanism of high-mannose N-glycan breakdown and metabolism by Bifidobacterium longum.Nature chemical biology · 2023Article
- Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1.Nature communications · 2022Article
- Impaired catabolism of free oligosaccharides due to MAN2C1 variants causes a neurodevelopmental disorder.American journal of human genetics · 2022Article
- Molecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1.The EMBO journal · 2021Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fungal α-mannosidase Ams1 and its mammalian homolog MAN2C1 hydrolyze terminal α-linked mannoses in free oligosaccharides released from misfolded glycoproteins or lipid-linked oligosaccharide donors. Ams1 is transported by selective autophagy into vacuoles. Here, we determine the tetrameric structure of Ams1 from the fission yeast Schizosaccharomyces pombe at 3.2 Å resolution by cryo-electron microscopy. Distinct from a low resolution structure of S. cerevisiae Ams1, S. pombe Ams1 has a prominent N-terminal tail that mediates tetramerization and an extra β-sheet domain. Ams1 shares a conserved active site with other enzymes in glycoside hydrolase family 38, to which Ams1 belongs, but contains extra N-terminal domains involved in tetramerization. The atomic structure of Ams1 reported here will aid understanding of its enzymatic activity and transport mechanism.
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