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Literature summary for 1.13.11.50 extracted from

  • Brkic, H.
    Insight of the iron binding and transport in Dke1 - A molecular dynamics study (2015), Croat. Chem. Acta, 88, 297-306 .
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamic simulations with wild-type and mutants E88Q, R80A, Y70A of the Fe2+ free protein, of the enzyme with Fe2+ bound in the active site, without and with applying random force, and of the proteins with the metal ion located at the entrance of the water tunnel Acinetobacter johnsonii

Protein Variants

Protein Variants Comment Organism
E98Q an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein Acinetobacter johnsonii
R80A mutation causes relocation of Glu11 from neighbor subunit closer to His104, enabling formation of the Glu11(OE1/2)-His104(NE2H/CD2H) H-bond Acinetobacter johnsonii
Y70A an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein Acinetobacter johnsonii

Metals/Ions

Metals/Ions Comment Organism Structure
Iron an interplay of residues Glu98, His104, Glu11 (from the neighbor subunit), and Arg80 is the most important for the Fe2+ transport in and out of the protein. The Fe2+ ion when expelled from the binding site can be trapped at different locations within the enzyme. The neighborhood of residue Glu11 (form the neighbor subunit) is the second most favorable binding site for the Fe2+ ion after the active site Acinetobacter johnsonii

Organism

Organism UniProt Comment Textmining
Acinetobacter johnsonii Q8GNT2
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Synonyms

Synonyms Comment Organism
acetylacetone-cleaving enzyme
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Acinetobacter johnsonii
Dke1
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Acinetobacter johnsonii