The abstract is read at the publisher; the summary is JClub's.
In mouse liver peroxisomes, urate oxidase homotetramers form helical fibers that tile into a stable porous lamellar scaffold, preserving accessible surface area.
- Why it matters: Cells must maintain metabolism in crowded intracellular space, but how supramolecular enzyme architectures affect function in vivo is unclear.
- What they did: Using in situ cryo-electron tomography, the authors mapped the high-order urate oxidase structure and used structure-guided perturbations to disrupt assembly in vivo.
- The result: Disrupting the assembly abolishes the scaffold without changing intrinsic catalytic activity and increases resistance to thermal, proteolytic, and oxidative stress, supporting robust sustained function in the peroxide-rich matrix.
The findingWhy it mattersWhat they didThe result
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