Fig. 4: cryo-EM structures of AGAL5 under different conditions. | Communications Chemistry

Fig. 4: cryo-EM structures of AGAL5 under different conditions.

From: Activity-based metaproteomics driven discovery and enzymological characterization of potential α-galactosidases in the mouse gut microbiome

Fig. 4

a Superposition of the electron density maps of native AGAL5 (light gray) and CaCl2 treated AGAL5 (blue). b Models from (a), highlighting structural differences, particularly the loops in CaCl2 treated AGAL5, which cannot be resolved. c Red circles mark the missing regions in CaCl2 treated AGAL5 in the zoom-in view of a protomer from (b). d The N-terminal, (β/α)8-barrel, and C-terminal domains of one protomer in the native AGAL5 tetramer model are highlighted, with the active site Asp480 shown as a sphere. e Another orientation of the native AGAL5 tetramer model, rotated 90° along with x axis. f Secondary structure and critical catalytic residue are labeled and numbered in a zoom-in view of the catalytic region ((β/α)8-barrel domain).

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