Pinho, Filipa G. and Romao, Celia V. and Pinto, Ana F. and Saraiva, Ligia M. and Huber, Harald and Matias, Pedro M. and Teixeira, Miguel and Bandeiras, Tiago M. (2010) Cloning, purification, crystallization and X-ray crystallographic analysis of Ignicoccus hospitalis neelaredoxin. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 66. pp. 605-607. ISSN 2053-230X,
Full text not available from this repository. (Request a copy)Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NANOARCHAEUM-EQUITANS; SUPEROXIDE REDUCTASES; SP-NOV; RESOLUTION; DISMUTASE; MECHANISM; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 30 Jul 2020 11:24 |
| Last Modified: | 30 Jul 2020 11:24 |
| URI: | https://pred.uni-regensburg.de/id/eprint/24743 |
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