24MP

Crystal structure of the GH134 mannanase from Aspergillus nidulans

Summary for 24MP

• Entry DOI: 10.2210/pdb24mp/pdb
• Descriptor: AnGH134, ETHANOL, N-PROPANOL, ... (4 entities in total)
• Functional Keywords: gh134; mannanase, carbohydrate
• Biological source: Aspergillus nidulans FGSC A4
• Total number of polymer chains: 2
• Total formula weight: 38522.22

Authors

Chen, S.C.,Hsu, C.H. (deposition date: 2026-03-11, release date: 2026-09-23)

Primary citation

Chen, S.C.,Kuo, P.C.,Chen, W.M.,Sheu, S.Y.,Huang, Y.B.,Huang, C.Y.,Chien, I.W.,Lee, T.H.,Hsu, C.H.
Structural Characterization and Engineering of a GH134 beta-Mannanase from Aspergillus nidulans for Enhancement of Activity and Stability.
J.Agric.Food Chem., 74:27687-27697, 2026

PubMed Abstract: Mannans are abundant plant hemicelluloses, and endo-β-mannanases are important biocatalysts for their conversion into functional manno-oligosaccharides. Here, we report the structural and functional characterization of a glycoside hydrolase family 134 β-mannanase from Aspergillus nidulans (AnGH134) and a structure-guided engineering strategy to improve its performance on locust bean gum. The 1.75 Å crystal structure reveals the conserved lysozyme-like fold of GH134 enzymes and supports an inverting catalytic mechanism with Glu43 and Asp55 as the putative catalytic residues. Docking, mutational, and molecular dynamics analyses indicate that AnGH134 uses an extended substrate-binding groove and that groove-exit residues and the C-terminal region contribute to productive catalysis. Guided by these findings, N-terminal fusion of CBM10 enhanced catalytic efficiency and thermal stability, whereas C-terminal fusion was detrimental. These results provide a framework for engineering GH134 mannanases.

PubMed: 42715962
DOI: 10.1021/acs.jafc.6c05159

Experimental method

X-RAY DIFFRACTION (1.75 Å)