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Literature summary for 1.15.1.1 extracted from

  • Banci, L.; Bertini, I.; Calderone, V.; Cramaro, F.; Del Conte, R.; Fantoni, A.; Mangani, S.; Quattrone, A.; Viezzoli, M.S.
    A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal (2005), Proc. Natl. Acad. Sci. USA, 102, 7541-7546.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of both solution and crystal structure of superoxide dismutase paralog lacking two Cu ligands and without enzymic activity. In solution, protein is monomeric. In crystal structure, it is well structured and organized in covalent dimers. Discussion of order/disorder transition Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Zn in solution, 1 mol per mol of protein. In crystal, a second Zn is bound at the interface between the two enzyme molecules leading to the formation of covalently bound enzyme dimers Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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superoxide dismutase paralog lacking two Cu ligands and without enzymic activity
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