6LZ1

Structure of S.pombe alpha-mannosidase Ams1

Summary for 6LZ1

• Entry DOI: 10.2210/pdb6lz1/pdb
• EMDB information: 30021
• Descriptor: Ams1, ZINC ION (2 entities in total)
• Functional Keywords: glycoside hydrolase, hydrolase
• Biological source: Schizosaccharomyces pombe 972h- (Fission yeast)
• Total number of polymer chains: 4
• Total formula weight: 517068.32

Authors

Zhang, J.,Ye, K. (deposition date: 2020-02-17, release date: 2020-09-09, Last modification date: 2024-03-27)

Primary citation

Zhang, J.,Wang, Y.Y.,Du, L.L.,Ye, K.
Cryo-EM structure of fission yeast tetrameric alpha-mannosidase Ams1.
Febs Open Bio, 10:2437-2451, 2020

PubMed 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.

PubMed: 32981237
DOI: 10.1002/2211-5463.12988

Experimental method

ELECTRON MICROSCOPY (3.2 Å)