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Literature summary for 1.1.98.6 extracted from

  • Logan, D.T.; Mulliez, E.; Larsson, K.M.; Bodevin, S.; Atta, M.; Garnaud, P.E.; Sj๖berg, B.M.; Fontecave, M.
    A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase (2003), Proc. Natl. Acad. Sci. USA, 100, 3826-3831.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
C-terminal region contains a Zn(Cys)4 center structurally related to the zinc ribbon motif and to rubredoxin and rubrerythrin. Residues Cys543, Cys546, Cys561, and Cys564 coordinate the metal ion tetrahedrally Tequatrovirus T4

Protein Variants

Protein Variants Comment Organism
C644A mutation in a residue of the Zn(Cys)4 center, almost complete loss of activity due to inability to generate the catalytically essential glycyl radical Escherichia coli
C647A mutation in a residue of the Zn(Cys)4 center, almost complete loss of activity due to inability to generate the catalytically essential glycyl radical Escherichia coli
C662A mutation in a residue of the Zn(Cys)4 center, almost complete loss of activity due to inability to generate the catalytically essential glycyl radical Escherichia coli
C665A mutation in a residue of the Zn(Cys)4 center, almost complete loss of activity due to inability to generate the catalytically essential glycyl radical Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn C-terminal region contains a Zn(Cys)4 center. Residues Cys543, Cys546, Cys561, and Cys564 coordinate the metal ion tetrahedrally Tequatrovirus T4
Zn2+ C-terminal region contains a Zn(Cys)4 center Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P28903
-
-
Tequatrovirus T4 P07071
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-