ArticleActa crystallographica. Section F, Structural biology communications2026
Structure of recombinant Thermoascus aurantiacus xylanase TaXyn10 with an authentic N-terminal pyroglutamate.
Article in Acta crystallographica. Section F, Structural biology communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The thermostable GH10 xylanase from Thermoascus aurantiacus (TaXyn10) is an industrially relevant enzyme whose native structure contains an N-terminal pyroglutamate (PCA) modification. Recombinant production of proteins containing an N-terminal PCA is often hindered by purification strategies that disrupt the authentic N-terminus. Here, we report the 1.1 Å resolution crystal structure of TaXyn10 recombinantly produced in Escherichia coli and purified using a split-intein-based system. The structure closely resembles that of the native protein. Electron-density maps support the presence of an intact N-terminal PCA, with partial occupancy consistent with spontaneous cyclization of the exposed N-terminal glutamine after intein cleavage. These results demonstrate that split-intein-based purification enables recovery of the native mature state of TaXyn10 and can preserve physiologically relevant N-terminal PCA formation in recombinant protein produced in E. coli.
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