ABSTRACT
To investigate the superoxide dismutase in extremthermoacidal environment,a reliable three-dimensional molecular structure of the protein encoded by the sod gene from Thermoplasma acidophilum was built.Evolutionary trace analysis of this protein detected 11 trace residues.Among them,the residues of Ash39,Gly105 and Glu162 were randomly scattered throughout the mapped structure;the other residues were all distinctly clusteredin a subgroup near Fe atom binding site.From these results,this gene encoded a Fe-depending superoxide dismutase based on the modeled structure;moreover,the detected trace residues around Fe atom might be directly responsible for Febinding and catalytic function.
ABSTRACT
To investigate the superoxide dismutase in extremthermoacidal environment,a reliable three-dimensional molecular structure of the protein encoded by the sod gene from Thermoplasma acidophilum was built.Evolutionary trace analysis of this protein detected 11 trace residues.Among them,the residues of Ash39,Gly105 and Glu162 were randomly scattered throughout the mapped structure;the other residues were all distinctly clusteredin a subgroup near Fe atom binding site.From these results,this gene encoded a Fe-depending superoxide dismutase based on the modeled structure;moreover,the detected trace residues around Fe atom might be directly responsible for Febinding and catalytic function.