9L3O

Crystal structure of endo-processive xyloglucanase Xeg5A from Aspergillus oryzae with XXLG

Summary for 9L3O

• Entry DOI: 10.2210/pdb9l3o/pdb
• Related: 9L3D 9L3J
• Descriptor: Glycoside hydrolase superfamily, beta-D-glucopyranose, DI(HYDROXYETHYL)ETHER, ... (13 entities in total)
• Functional Keywords: xyloglucanase, complex, hydrolase
• Biological source: Aspergillus oryzae RIB40
• Total number of polymer chains: 2
• Total formula weight: 155234.21

Authors

Nakamichi, Y.,Shimada, N.,Watanabe, M.,Fujii, T.,Matsuzawa, T. (deposition date: 2024-12-19, 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

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: 40414580
DOI: 10.1016/j.jsb.2025.108213

Experimental method

X-RAY DIFFRACTION (2 Å)