Cloned (Comment) | Organism |
---|---|
- |
Staphylococcus aureus |
Crystallization (Comment) | Organism |
---|---|
inactive N7A variant of IsdG in complex with Fe3+-protoporphyrin IX, to 1.8 A resolution. The metalloporphyrin is buried into a deep clefts such that the propionic acid forms salt bridges to two Arg residues. His77, a critical residue required for activity, is coordinated to the Fe3+ atom. The bound porphyrin ring forms extensive steric interactions in the binding cleft such that the ring is highly distorted from the plane. This distortion is best described as ruffled and places the beta- and delta-meso carbons proximal to the distal oxygen-binding site. In the IsdG-hemin structure, Fe3+ is pentacoordinate, and the distal side is occluded by the side chain of Ile55 | Staphylococcus aureus |
isoform IsdI in complex with cobalt protoporphyrin IX, to 1.8 A resolution. The metalloporphyrin is buried into a deep cleft such that the propionic acid forms salt bridges to two Arg residues. His76, a critical residue required for activity, is coordinated to the Co3+ atom. The bound porphyrin ring forms extensive steric interactions in the binding cleft such that the ring is highly distorted from the plane. This distortion is best described as ruffled and places the beta- and delta-meso carbons proximal to the distal oxygen-binding site. in the structure of IsdI-cobalt protoporphyrin IX, the distal side of the cobalt protoporphyrin IX accommodates a chloride ion in a cavity formed through a conformational change in Ile55. The chloride ion participates in a hydrogen bond to the side chain amide of Asn6 | Staphylococcus aureus |
Protein Variants | Comment | Organism |
---|---|---|
N7A | inactive | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | Q7A649 | isoform IsdG | - |
Staphylococcus aureus | Q7A827 | isoform IsdI | - |
Synonyms | Comment | Organism |
---|---|---|
isdG | - |
Staphylococcus aureus |
isdI | - |
Staphylococcus aureus |