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Literature summary for 1.11.1.5 extracted from

  • Dias, J.M.; Alves, T.; Bonifacio, C.; Pereira, A.S.; Trincao, J.; Bourgeois, D.; Moura, I.; Romao, M.J.
    Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617 (2004), Structure, 12, 961-973.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
the enzyme crystallizes in two different forms obtained at pH 4 and pH 5.3, corresponding to form IN, inactive, and OUT, active. In the form OUT, the calcium binding site is fully occupied by Ca2+, coordinated by seven ligands in a distorted pentagonal bipyramidal geometry, and four water molecules Marinobacter nauticus

Organism

Organism UniProt Comment Textmining
Marinobacter nauticus
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Purification (Commentary)

Purification (Comment) Organism
four-step purification protocol Marinobacter nauticus

Subunits

Subunits Comment Organism
dimer the dimer is stabilized by hydrophobic interactions between both C-terminal coiled coils of the two monomers. There are also hydrophobic interactions among residues 39-66. The presence of Ca2+ triggers conformational changes, which contribute to stronger interactions within the dimer Marinobacter nauticus