9L3J
Crystal structure of endo-processive xyloglucanase Xeg5A from Aspergillus oryzae with GXG
Summary for 9L3J
| Entry DOI | 10.2210/pdb9l3j/pdb |
| Related | 9L3D |
| Descriptor | Glycoside hydrolase superfamily, alpha-D-mannopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total) |
| Functional Keywords | xyloglucanase, complex, hydrolase |
| Biological source | Aspergillus oryzae RIB40 |
| Total number of polymer chains | 2 |
| Total formula weight | 151893.59 |
| Authors | Nakamichi, Y.,Shimada, N.,Watanabe, M.,Fujii, T.,Matsuzawa, T. (deposition date: 2024-12-18, release date: 2025-06-25) |
| Primary citation | Nakamichi, Y.,Shimada, N.,Watanabe, M.,Fujii, T.,Yaoi, K.,Matsuzawa, T. Structural insights into substrate recognition of tri-modular xyloglucanase from Aspergillus oryzae. J.Struct.Biol., 217:108213-108213, 2025 Cited by PubMed Abstract: Xeg5A from Aspergillus oryzae belongs to glycoside hydrolase family 5 subfamily 4. This enzyme has been characterized as a xyloglucan-specific endo-β-1,4-glucanase (xyloglucanase) that cleaves the main chain of xyloglucan at both unbranched and xylosylated glucosyl residues in an endo-processive mode of action. X-ray crystallography revealed that Xeg5A is a tri-modular enzyme composed of a catalytic, an Ig-like, and a C-terminal CBM46-like domains. Xeg5A structures complexed with branched xyloglucan oligosaccharides at subsites -4 to +4 showed that the recognition of xyloglucan side-chain moieties is important for Xeg5A activity. The crystal structure also provided structural insights into the role of the CBM46-like domain in contributing to regiospecificity and, possibly, processivity. PubMed: 40414580DOI: 10.1016/j.jsb.2025.108213 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.74 Å) |
Structure validation
Download full validation report
