6PT7

Structure of KatE1 catalase from Acinetobacter sp. Ver3

Summary for 6PT7

• Entry DOI: 10.2210/pdb6pt7/pdb
• Descriptor: Catalase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• Functional Keywords: catalase, peroxide, nadp, cold-adapted, oxidoreductase
• Biological source: Acinetobacter sp. Ver3
• Total number of polymer chains: 1
• Total formula weight: 58156.62

Authors

Gonzalez, J.M.,Sartorio, M.G.,Cortez, N. (deposition date: 2019-07-15, release date: 2020-07-22, Last modification date: 2025-11-12)

Primary citation

Sartorio, M.G.,Cortez, N.,Gonzalez, J.M.
Structure and functional properties of the cold-adapted catalase from Acinetobacter sp. Ver3 native to the Atacama plateau in northern Argentina.
Acta Crystallogr D Struct Biol, 77:369-379, 2021

PubMed Abstract: 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.

PubMed: 33645540
DOI: 10.1107/S2059798321000929

Experimental method

X-RAY DIFFRACTION (2.15 Å)