Structure of recombinant Thermoascus aurantiacus xylanase TaXyn10 with an authentic N-terminal pyroglutamate

Abstract

The high-resolution structure of the T. aurantiacus xylanase TaXyn10 expressed in Escherichia coli shows that recombinant production combined with split-intein-based purification recovers the native fold of TaXyn10 and permits the formation of an N-terminal pyroglutamate. These results demonstrate that this approach can enable recombinant proteins to adopt their native mature state in E. coli, including physiologically relevant post-translational modifications such as N-terminal pyroglutamate formation.