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Literature summary for 1.16.3.1 extracted from

  • Haikarainen, T.; Tsou, C.C.; Wu, J.J.; Papageorgiou, A.C.
    Crystal structures of Streptococcus pyogenes Dpr reveal a dodecameric iron-binding protein with a ferroxidase site (2010), J. Biol. Inorg. Chem., 15, 183-194.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Streptococcus pyogenes

Crystallization (Commentary)

Crystallization (Comment) Organism
determination of the crystal structure of Streptococcus pyogenes Dpr in iron-free and iron-bound form at 2.0 and 1.93 A resolution, respectively Streptococcus pyogenes

Protein Variants

Protein Variants Comment Organism
D66A site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation Streptococcus pyogenes
D77A site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation Streptococcus pyogenes
E81A site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation Streptococcus pyogenes
H50A site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation Streptococcus pyogenes
H62A site-directed mutagenesis in the active-site reveals a dramatic decrease in iron incorporation Streptococcus pyogenes

Organism

Organism UniProt Comment Textmining
Streptococcus pyogenes Q99YU7
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Subunits

Subunits Comment Organism
dodecamer bending magnet macromolecular crystallography Streptococcus pyogenes

Synonyms

Synonyms Comment Organism
Dpr DNA-binding protein from starved cells Streptococcus pyogenes

General Information

General Information Comment Organism
physiological function binding and oxidization of iron, thus preventing the formation of harmful reactive oxygen species Streptococcus pyogenes