TY - JOUR
T1 - Cloning, purification, crystallization and X-ray crystallographic analysis of Ignicoccus hospitalis neelaredoxin
AU - Teixeira, Miguel Nuno
AU - Teixeira, Ligia Raquel
AU - Matias, Pedro Manuel
N1 - Romao, Celia V.; Pinto, Ana F. (ITQB)
PY - 2010/1/1
Y1 - 2010/1/1
N2 - Superoxide reductases (SORs) are metalloproteins which constitute the most recently identified oxygen-detoxification system in anaerobic and microaerobic bacteria and archaea. SORs are involved in scavenging superoxide radicals from the cell by catalyzing the reduction of superoxide (O-2(center dot-)) to hydrogen peroxide and are characterized by a catalytic nonhaem iron centre coordinated by four histidine ligands and one cysteine ligand. Ignicoccus hospitalis, a hyperthermophilic crenarchaeon, is known to have a neelaredoxin-type SOR that keeps toxic oxygen species levels under control. Blue crystals of recombinant I. hospitalis oxidized neelaredoxin (14.1 kDa, 124 residues) were obtained. These crystals diffracted to 2.4 angstrom resolution in-house at room temperature and belonged to the hexagonal space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 108, c = 64 angstrom. Cell-content analysis indicated the presence of one monomer in the asymmetric unit.
AB - Superoxide reductases (SORs) are metalloproteins which constitute the most recently identified oxygen-detoxification system in anaerobic and microaerobic bacteria and archaea. SORs are involved in scavenging superoxide radicals from the cell by catalyzing the reduction of superoxide (O-2(center dot-)) to hydrogen peroxide and are characterized by a catalytic nonhaem iron centre coordinated by four histidine ligands and one cysteine ligand. Ignicoccus hospitalis, a hyperthermophilic crenarchaeon, is known to have a neelaredoxin-type SOR that keeps toxic oxygen species levels under control. Blue crystals of recombinant I. hospitalis oxidized neelaredoxin (14.1 kDa, 124 residues) were obtained. These crystals diffracted to 2.4 angstrom resolution in-house at room temperature and belonged to the hexagonal space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 108, c = 64 angstrom. Cell-content analysis indicated the presence of one monomer in the asymmetric unit.
KW - MECHANISM
KW - SP-NOV
KW - DISMUTASE
KW - NANOARCHAEUM-EQUITANS
KW - SUPEROXIDE REDUCTASES
KW - RESOLUTION
U2 - 10.1107/s1744309110012030
DO - 10.1107/s1744309110012030
M3 - Article
VL - 66
SP - 605
EP - 607
JO - Acta Crystallographica Section F-Structural Biology And Crystallization Com
JF - Acta Crystallographica Section F-Structural Biology And Crystallization Com
SN - 1744-3091
IS - Part 5
ER -