Crystallization (Comment) | Organism |
---|---|
crystals of the H327A mutants are obtained by vapour diffusion technique. Crystals of H369A are obtained by mixing equal volumes of a reservoir solution containing 11.5% PEG 6000, 0.2 M imidazole/malate, pH 6.5, and of protein, in presence or not of 50 mM potassium nitrite and 50 mM sodium ascorbate. Crystals belong to space group P4(1)2(1)2 with cell dimensions a = b = 94.7 A, c = 159.9 A. The three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure | Pseudomonas aeruginosa |
Protein Variants | Comment | Organism |
---|---|---|
H327A | the three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure | Pseudomonas aeruginosa |
H369A | the three-dimensional structures of NIR mutant H327A, and H369A in complex with NO solved by multiple wave-length anomalous dispersion, using the iron anomalous signal, and molecular replacement techniques. In both refined crystal structures the c-heme domain, whilst preserving its classical c-type cytochrome fold, has undergone a 60° rigid-body rotation around an axis parallel with the pseudo 8-fold axis of the beta-propeller, and passing through residue Gln115. Even though the distance between the Fe ions of the c and d1-heme remains 21 A, the edge-to-edge distance between the two hemes has increased by 5 A. Furthermore the distal side of the d1-heme pocket appears to have undergone structural re-arrangement and Tyr10 has moved out of the active site. In the H369A-NO complex, the position and orientation of NO is significantly different from that of the NO bound to the reduced wild-type structure | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | - |
mutant H327A | - |
Synonyms | Comment | Organism |
---|---|---|
NiR | - |
Pseudomonas aeruginosa |
NiR-Pa | - |
Pseudomonas aeruginosa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme c | - |
Pseudomonas aeruginosa | |
Heme d1 | - |
Pseudomonas aeruginosa |