Engineering the pattern of protein glycosylation modulates the thermostability of a GH11 xylanase.

ABSTRACT: Protein glycosylation is a common post-translational modification, the effect of which on protein conformational and stability is incompletely understood. Here we have investigated the effects of glycosylation on the thermostability of Bacillus subtilis xylanase A (XynA) expressed in Pichia pastoris. Intact mass analysis of the heterologous wild-type XynA revealed two, three, or four Hex(8-16)GlcNAc2 modifications involving asparagine residues at positions 20, 25, 141, and 181. Molecular dynamics (MD) simulations of the XynA modified with various combinations of branched Hex9GlcNAc2 at these positions indicated a significant contribution from protein-glycan interactions to the overall energy of the glycoproteins. The effect of glycan content and glycosylation position on protein stability

SUBMITTER: Fonseca-Maldonado R 

PROVIDER: S-EPMC3757213 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature