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TitleCryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.
Journal, issue, pagesFEBS Open Bio, Vol. 10, Issue 11, Page 2437-2451, Year 2020
Publish dateOct 20, 2020
AuthorsJianxiu Zhang / Ying-Ying Wang / Li-Lin Du / Keqiong Ye /
PubMed AbstractFungal 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. ...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.
External linksFEBS Open Bio / PubMed:32981237 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

30021

6lz1

EMDB-30021, PDB-6lz1:
Structure of S.pombe alpha-mannosidase Ams1
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • Schizosaccharomyces pombe (fission yeast)
  • schizosaccharomyces pombe 972h- (yeast)
KeywordsHYDROLASE / glycoside hydrolase

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