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Structure paper

TitleAn enzyme's metal preference evolves through redox modulation driven by the cofactor's secondary coordination sphere.
Journal, issue, pagesMol. Biol. Evol., Vol. 43, Year 2026
Publish dateJan 14, 2026 (structure data deposition date)
AuthorsMackenzie, E.S. / Sendra, K.M. / Basle, A. / Mazgaj, R. / Kehl-Fie, T.E. / Waldron, K.J.
External linksMol. Biol. Evol. / PubMed:41684149
MethodsX-ray diffraction
Resolution1.4 - 2 Å
Structure data

PDB-9tw9:
Legionella monocytogenes SodA wt
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-9twa:
Legionella monocytogenes SodA mutant GL to VI
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-9twc:
Legionella monocytogenes SodA wt
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-HOH:
WATER

Source
  • listeria monocytogenes (bacteria)
  • neisseria gonorrhoeae (bacteria)
KeywordsOXIDOREDUCTASE / superoxide dismutase / SOD / redox / metalloenzyme / protein evolution

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