RESUMO
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.
RESUMO
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.
RESUMO
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.
RESUMO
Beta2 adrenergic receptor (β2 AR) is one member of G protein coupled receptors (GPCRs), which is a key pharmaceutical target in the treatment of asthma. Evolutionary trace (ET) method was employed to analyze AR sequences and 44 conserved residues were identified. Then molecular dynamics (MD) simulation of the β2 wild-type receptor, D130N active mutant and D79N inactive mutant were carried out and tried to explore the structural/dynamic features characterizing functionally different states of the receptor,by means of investigating ET identified conserved basic residues in the wild-type receptor and its two mutants. Particularly, it was found that the departing of D130 from R131 of DRY motif and approaching to K149 are highly correlated with the receptor activation,and the movement of helix 2, 4 and 6 upon receptor activation is inferred from the observation that R151 and K270 interact with other residues in the receptor active state on the basis of little change of the side chain orientations. The results might provide further insights into the activating mechanism of β2 AR mutants, as well as the molecular bases of the diseases induced by the mutations of the receptor.