6lz1

Publication Abstract from PubMed

Fungal alpha-mannosidase Ams1 and its mammalian homolog MAN2C1 hydrolyze terminal alpha-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 A 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 beta-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.

Cryo-EM structure of fission yeast tetrameric alpha-mannosidase Ams1.,Zhang J, Wang YY, Du LL, Ye K FEBS Open Bio. 2020 Sep 27. doi: 10.1002/2211-5463.12988. PMID:32981237^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.