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-Structure paper
タイトル | Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1. |
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ジャーナル・号・ページ | FEBS Open Bio, Vol. 10, Issue 11, Page 2437-2451, Year 2020 |
掲載日 | 2020年10月20日 |
![]() | Jianxiu Zhang / Ying-Ying Wang / Li-Lin Du / Keqiong Ye / ![]() |
PubMed 要旨 | 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. ...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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手法 | EM (単粒子) |
解像度 | 3.2 Å |
構造データ | EMDB-30021, PDB-6lz1: |
化合物 | ![]() ChemComp-ZN: |
由来 |
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![]() | HYDROLASE / glycoside hydrolase |