Observed surface lysine acetylation of human carbonic anhydrase II expressed in Escherichia coli.

ABSTRACT: Acetylation of surface lysine residues of proteins has been observed in Escherichia coli (E. coli), an organism that has been extensively utilized for recombinant protein expression. This post-translational modification is shown to be important in various processes such as metabolism, stress-response, transcription, and translation. As such, utilization of E. coli expression systems for protein production may yield non-native acetylation events of surface lysine residues. Here we present the crystal structures of wild-type and a variant of human carbonic anhydrase II (hCA II) that have been expressed in E. coli and exhibit surface lysine acetylation and we speculate on the effect this has on the conformational stability of each enzyme. Both structures were determined to 1.6 Å resolution an

SUBMITTER: Mahon BP 

PROVIDER: S-EPMC4622213 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature