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The β-hairpin effect: Structural insights into bacterial laccase function and stability.

Leticia León-Luna¹, Paloma Gil-Rodríguez¹, Enrique Rudiño-Piñera¹

¹Laboratorio de Bioquímica Estructural, Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México (UNAM), Morelos, Mexico.

International Journal of Biological Macromolecules

|February 14, 2026

Summary

Deleting a specific β-hairpin in bacterial laccase (TthMCO) expands its pH activity range and improves substrate binding. However, this modification negatively impacts overall reaction speed, revealing the hairpin

Keywords:

Multicopper oxidase Structural dynamics Thermus thermophilus laccase pH-dependent conformational change Β-Hairpin motif

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Area of Science:

Enzymology
Biochemistry
Structural Biology

Background:

Laccases are multicopper oxidases with industrial applications.
The Thermus thermophilus HB27 laccase (TthMCO) features a unique methionine-rich motif and a β-hairpin structure.
This β-hairpin partially blocks solvent access to the T1 copper site, potentially affecting enzyme activity.

Purpose of the Study:

To investigate the role of the β-hairpin in TthMCO's catalytic activity and pH dependence.
To engineer TthMCO variants by deleting the β-hairpin to mimic fungal laccase architecture.
To understand the structural and functional implications of β-hairpin removal.

Main Methods:

Generation of two deletion variants: ∆1 (removing mobile regions) and ∆2 (deleting the entire β-hairpin).
Crystallography to assess structural integrity of variants.
Kinetic analysis and pH profiling to determine catalytic parameters and pH-dependent activity.

Main Results:

Deletion of the β-hairpin expanded the pH range for enzymatic activity.
The K_m values of the deletion variants were improved, indicating better substrate binding.
Overall reaction velocity (k_cat) was negatively affected by the β-hairpin deletion.

Conclusions:

The β-hairpin in TthMCO is crucial for balancing substrate accessibility and electron-transfer efficiency.
Deletion of the β-hairpin provides insights into rational engineering of bacterial laccases.
This study offers fundamental understanding for optimizing laccase function in industrial settings.