A new crystal form of GABARAPL2

This article reports a new, untwinned GABARAPL2 crystal form, also in space group P21, but with a 98 ° monoclinic angle. No major conformational differences were observed between the structures. In the structure described here, the C-terminal Phe117 binds into the LIR docking site (LDS) of a neighbouring molecule within the asymmetric unit, as observed in the previously reported structure. This crystal contact blocks the LDS for co-crystallization with ligands. Phe117 of GABARAPL2 is normally removed during biological processing by Atg4 family proteases. These data indicate that to establish interactions with the LIR, Phe117 should be removed to eliminate the crystal contact and liberate the LDS for co-crystallization with LIR peptides.

Source: Acta Crystallographica Section F - April 30, 2021 Category: Biochemistry Authors: Scicluna, K. Dewson, G. Czabotar, P.E. Birkinshaw, R.W. Tags: GABARAPL2 GATE-16 Atg8 autophagy autophagosome LIR LC3 research communications Source Type: research