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Literature summary extracted from

  • Havukainen, H.; Haataja, S.; Kauko, A.; Pulliainen, A.T.; Salminen, A.; Haikarainen, T.; Finne, J.; Papageorgiou, A.C.
    Structural basis of the zinc- and terbium-mediated inhibition of ferroxidase activity in Dps ferritin-like proteins (2008), Protein Sci., 17, 1513-1521.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.16.3.1 in complex with zinc and terbium, at 1.8 A and 2.1 A resolution, respectively. Both ions bind to the ferroxidase center in the same location as iron Listeria innocua

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.16.3.1 terbium above 0.2 mM, complete abolition of iron binding. Crystal structure of enzyme complex at 2.1 A resolution, terbium binds to the ferroxidase center Listeria innocua
1.16.3.1 Zinc above 0.2 mM, complete abolition of iron binding. Crystal structure of enzyme complex at 1.8 A resolution, zinc binds to the ferroxidase center. Residues H40 and H44 form a zinc-binding site present in all known Streptococcus suis Dpr variants and in Streptococcus pneumoniae, Streptococcus gordonii, and Streptococcus sanguinis Dpr proteins Listeria innocua
1.16.3.1 Zinc residues H40 and H44 form a zinc-binding site present in all known Streptococcus suis Dpr variants and in Streptococcus pneumoniae, Streptococcus gordonii, Listeria innocua, and Streptococcus sanguinis Dpr proteins Streptococcus gordonii
1.16.3.1 Zinc residues H40 and H44 form a zinc-binding site present in all known Streptococcus suis Dpr variants and in Streptococcus pneumoniae, Streptococcus gordonii, Listeria innocua, and Streptococcus sanguinis Dpr proteins Streptococcus pneumoniae
1.16.3.1 Zinc residues H40 and H44 form a zinc-binding site present in all known Streptococcus suis Dpr variants and in Streptococcus pneumoniae, Streptococcus gordonii, Listeria innocua, and Streptococcus sanguinis Dpr proteins Streptococcus sanguinis
1.16.3.1 Zinc residues H40 and H44 form a zinc-binding site present in all known Streptococcus suis Dpr variants and in Streptococcus pneumoniae, Streptococcus gordonii, Listeria innocua, and Streptococcus sanguinis Dpr proteins Streptococcus suis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.16.3.1 Iron
-
 Streptococcus pneumoniae
1.16.3.1 Iron
-
 Streptococcus sanguinis
1.16.3.1 Iron
-
 Streptococcus gordonii
1.16.3.1 Iron
-
 Streptococcus suis
1.16.3.1 Iron
-
 Listeria innocua

Organism

EC Number Organism UniProt Comment Textmining
1.16.3.1 Listeria innocua P80725
-
-
1.16.3.1 Streptococcus gordonii
-
-
-
1.16.3.1 Streptococcus pneumoniae
-
-
-
1.16.3.1 Streptococcus sanguinis
-
-
-
1.16.3.1 Streptococcus suis
-
-
-

Synonyms

EC Number Synonyms Comment Organism
1.16.3.1 Dps protein
-
 Streptococcus pneumoniae
1.16.3.1 Dps protein
-
 Streptococcus gordonii
1.16.3.1 Dps protein
-
 Streptococcus suis
1.16.3.1 Dps protein
-
 Listeria innocua