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Structure Modeling and Evolutionary Trace Analysis of Superoxide Dismutase from Extremophile Thermoplasma Acidophilum / 现代生物医学进展
Progress in Modern Biomedicine ; (24): 1057-1060, 2008.
Article in Zh | WPRIM | ID: wpr-498907
Responsible library: WPRO
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.
Key words
Full text: 1 Index: WPRIM Language: Zh Journal: Progress in Modern Biomedicine Year: 2008 Type: Article
Full text: 1 Index: WPRIM Language: Zh Journal: Progress in Modern Biomedicine Year: 2008 Type: Article