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Figure 4
Comparison with known H2O2-soaked MnSOD structures in the PDB. Structural comparisons of H2O2-treated human Gln143Asn MnSOD (purple) with (a) human (yellow; PDB entry 8vj5) and (b) E. coli (orange; PDB entry 3k9s) wild-type enzymes, as well as with (c) the product-inhibited MnSOD variants Trp161Phe (cyan, neutron, PDB entry 8vhw) and Tyr34Phe (red, neutron, PDB entry 9bvy). We observe H2O2 binding in the pre-established LIG and PEO binding sites, with subtle differences, potentially owing to the Gln143 mutation-induced cavity. Notably, Tyr34 samples a shifted conformation (∼80% occupancy) in this cavity, drawing closer to both the LIG H2O2 and His30. This conformational flexibility is not typically observed in wild-type or other variants lacking this mutation-induced cavity between the metal primary sphere and the second-shell solvent gateway.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 81| Part 11| November 2025| Pages 467-477
https://doi.org/10.1107/S2053230X25009045
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