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November 2025 issue
Cover illustration: The Gln143Asn mutant of human mitochondrial manganese superoxide dismutase is kinetically slow and catalytically impaired. The increased distance of Asn from WAT1 disrupts critical proton-coupled electron-transfer events, and the redox cycling of the active-site metal is impaired. This stalls the electrostatic cycling of positive charge on the enzyme surface and leads to the observation of transient H2O2-bound states in this variant [Dasgupta et al. (2025), Acta Cryst. F81, 467–477].
research communications
Mouse ketohexokinase A undergoes a conformational change during the catalytic cycle. The conformational change is consistent between the two isozymes, A and C, and across species.
PDB reference: mouse ketohexokinase A without ligand, 9p6q
We present the first detailed structure of a newly discovered fucosidase that has been shown to remove terminal fucose from fucoidan, uncovering unique features that set it apart from other known fucosidases and suggesting functional diversity among its homologs.
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A high-resolution X-ray structure of a Gln143Asn variant of manganese superoxide dismutase (MnSOD) reveals multiple hydrogen peroxide-binding sites beyond the canonical LIG and PEO binding positions within the active site. These findings expand the known landscape of product peroxide-bound states in MnSOD.
methods communications
Open access
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A device and method for gentle, automated and inexpensive solution exchange for macromolecular crystals is described.
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