Structure and functional properties of the cold-adapted catalase from Acinetobacter sp. Ver3 native to the Atacama plateau in northern Argentina
| Autor: | Mariana G. Sartorio, Néstor Cortez, Javier M. González |
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| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Protein Conformation Acclimatization Argentina Heme Crystallography X-Ray 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Structural Biology Enzyme Stability Hydrogen peroxide 030304 developmental biology 0303 health sciences Binding Sites Methionine Acinetobacter biology 030306 microbiology Thermophile Catalase biology.organism_classification Cold Temperature Salinity chemistry Biochemistry biology.protein NADP Mesophile |
| Zdroj: | Acta Crystallographica Section D Structural Biology. 77:369-379 |
| ISSN: | 2059-7983 |
| DOI: | 10.1107/s2059798321000929 |
| Popis: | Heme catalases remove hydrogen peroxide by catalyzing its dismutation into water and molecular oxygen, thereby protecting the cell from oxidative damage. The Atacama plateau in northern Argentina, located 4000 m above sea level, is a desert area characterized by extreme UV radiation, high salinity and a large temperature variation between day and night. Here, the heme catalase KatE1 from an Atacama Acinetobacter sp. isolate was cloned, expressed and purified, with the aim of investigating its extremophilic properties. Kinetic and stability assays indicate that KatE1 is maximally active at 50°C in alkaline media, with a nearly unchanged specific activity between 0°C and 40°C in the pH range 5.5–11.0. In addition, its three-dimensional crystallographic structure was solved, revealing minimal structural differences compared with its mesophilic and thermophilic analogues, except for a conserved methionine residue on the distal heme side, which is proposed to comprise a molecular adaptation to oxidative damage. |
| Databáze: | OpenAIRE |
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