31CT
Structure of recombinant Thermoascus aurantiacus xylanase TaXyn10 with an N-terminal pyroglutamate
Summary for 31CT
| Entry DOI | 10.2210/pdb31ct/pdb |
| Descriptor | Endo-1,4-beta-xylanase, GLYCEROL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | xylanase, pyroglutamate, hydrolase |
| Biological source | Thermoascus aurantiacus |
| Total number of polymer chains | 1 |
| Total formula weight | 33230.99 |
| Authors | Lennartz, F.,Weiss, M.S.,Mijatovic, J. (deposition date: 2026-05-26, release date: 2026-07-01, Last modification date: 2026-10-14) |
| Primary citation | Mijatovic, J.,Mueller, U.,Weiss, M.S.,Lennartz, F. Structure of recombinant Thermoascus aurantiacus xylanase TaXyn10 with an authentic N-terminal pyroglutamate. Acta Crystallogr.,Sect.F, 82:329-335, 2026 Cited by PubMed 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. PubMed: 42771010DOI: 10.1107/S2053230X26009155 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.11 Å) |
Structure validation
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