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裂殖酵母四聚体α-甘露糖苷酶 Ams1 的冷冻电镜结构

Cryo-EM structure of fission yeast tetrameric α-mannosidase Ams1.

机构信息

Key Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.

University of Chinese Academy of Sciences, Beijing, China.

出版信息

FEBS Open Bio. 2020 Nov;10(11):2437-2451. doi: 10.1002/2211-5463.12988. Epub 2020 Oct 20.

DOI:10.1002/2211-5463.12988
PMID:32981237
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7609781/
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.

摘要

真菌α-甘露糖苷酶 Ams1 及其哺乳动物同源物 MAN2C1 可水解从错误折叠糖蛋白或脂连接寡糖供体中释放的游离寡糖末端的α-连接甘露糖。Ams1 通过选择性自噬被转运到液泡中。在这里，我们通过冷冻电子显微镜以 3.2Å 的分辨率确定了裂殖酵母 Schizosaccharomyces pombe 中 Ams1 的四聚体结构。与低分辨率的酿酒酵母 Ams1 结构不同，S. pombe Ams1 具有一个突出的 N 端尾巴，介导四聚化和一个额外的β-折叠结构域。Ams1 与属于糖苷水解酶家族 38 的其他酶共享一个保守的活性位点，但包含额外的参与四聚化的 N 端结构域。这里报道的 Ams1 的原子结构将有助于理解其酶活性和运输机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/27f824ce442b/FEB4-10-2437-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/6f354e2bab5d/FEB4-10-2437-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/d9d898431755/FEB4-10-2437-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/67d1bfd80bb4/FEB4-10-2437-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/944d6b2e4ec6/FEB4-10-2437-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/917fe7a3ba15/FEB4-10-2437-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/2564f8fd2257/FEB4-10-2437-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/f2bf1ac4b010/FEB4-10-2437-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/27f824ce442b/FEB4-10-2437-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/6f354e2bab5d/FEB4-10-2437-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/d9d898431755/FEB4-10-2437-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/67d1bfd80bb4/FEB4-10-2437-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/944d6b2e4ec6/FEB4-10-2437-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/917fe7a3ba15/FEB4-10-2437-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/2564f8fd2257/FEB4-10-2437-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/f2bf1ac4b010/FEB4-10-2437-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b1ca/7609781/27f824ce442b/FEB4-10-2437-g008.jpg

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