Crystallization (Comment) | Organism |
---|---|
to 1.5 A resolution. Structure of the enzyme resembles the ferredoxin-like fold and forms a beta-barrel at the dimer interface. Two large pockets found on the outside of the barrel contain the putative active sites | Staphylococcus aureus |
Protein Variants | Comment | Organism |
---|---|---|
F23A | mutation does not significantly affect heme binding or degradation | Staphylococcus aureus |
H77A | mutation abolishes IsdG-mediated heme degradation | Staphylococcus aureus |
L17A | mutation does not significantly affect heme binding or degradation | Staphylococcus aureus |
M38A | slight reduction of heme degradation, mutation shifts the peak absorbance of the Soret band to 430 nm | Staphylococcus aureus |
N7A | mutation abolishes IsdG-mediated heme degradation | Staphylococcus aureus |
S70A | mutation does not significantly affect heme binding or degradation | Staphylococcus aureus |
W67A | mutation abolishes IsdG-mediated heme degradation | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | Q8NX62 | isoform IsdG | - |
Staphylococcus aureus | Q99X56 | isoform IsdI | - |
Staphylococcus aureus ATCC 700699 | Q99X56 | isoform IsdI | - |
Staphylococcus aureus MW2 | Q8NX62 | isoform IsdG | - |