Sandbox Reserved 1508: Difference between revisions

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== ~~'''~~Background~~'''~~

== Background==

:In oxidative stress, the organism manage to do a reduction of peroxides. This reaction is catalyzed by the peroxiredoxins. From a structural point of view, a specific amino acid is involved in this reaction: its a nucleophilic cystein, called peroxidatic cystein. In order to understand the mechanism and the specificity of this reaction according to its specific chemical environment, researchers used the ''Mycobacterium tuberculosis'' alkyl hydroperoxide reductase E (MtAhpE) as model (Pedre et al, 2016). The mutational effects of key residues in its environment are located in the active site. These amino acids create an environment favorising the reaction with peroxides.

In oxidative stress, the organism manage to do a reduction of peroxides. This reaction is catalyzed by the peroxiredoxins. From a structural point of view, a specific amino acid is involved in this reaction: its a nucleophilic cystein, called peroxidatic cystein. In order to understand the mechanism and the specificity of this reaction according to its specific chemical environment, researchers used the ''Mycobacterium tuberculosis'' alkyl hydroperoxide reductase E (MtAhpE) as model (Pedre et al, 2016). The mutational effects of key residues in its environment are located in the active site. These amino acids create an environment favorising the reaction with peroxides.

Peroxiredoxins are peroxidases which catalyze the reduction of peroxides (organic peroxide H2O2 or organic hydroperoxides).</div>

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According to PDB code 5C04, the structure of the protein has been characterized thanks to crystallography (X-Ray diffraction). The scientists obtained a resolution of 1.45 Å, a R-value free of 0.198 and a R-value work of 0.166. The structure of the 5C04 protein has in total 2 chains (A and B) represented by one sequence-unique entity (one polymer) of L-type polypeptide. Its length is 153 residues. Its secondary structure shows that 27% of alpha helix are composed by six helix for a total of 42 residues; and 27% of beta sheet are composed by 11 strands for also a total of 42 residues.

[[Image:sequence.png]]

''Sequence of the 5C04 protein''

[[Image:~~sequence view chain~~.png]]

[[Image:seq2.png]]

''Sequence view chain''

== Catalytic site ==

Sandbox Reserved 1508: Difference between revisions

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@@ Line 7: / Line 7: @@
-== '''Background'''
+== Background==
-:In oxidative stress, the organism manage to do a reduction of peroxides. This reaction is catalyzed by the peroxiredoxins. From a structural point of view, a specific amino acid is involved in this reaction: its a nucleophilic cystein, called peroxidatic cystein. In order to understand the mechanism and the specificity of this reaction according to its specific chemical environment, researchers used the ''Mycobacterium tuberculosis'' alkyl hydroperoxide reductase E (MtAhpE) as model (Pedre et al, 2016). The mutational effects of key residues in its environment are located in the active site. These amino acids create an environment favorising the reaction with peroxides.
+In oxidative stress, the organism manage to do a reduction of peroxides. This reaction is catalyzed by the peroxiredoxins. From a structural point of view, a specific amino acid is involved in this reaction: its a nucleophilic cystein, called peroxidatic cystein. In order to understand the mechanism and the specificity of this reaction according to its specific chemical environment, researchers used the ''Mycobacterium tuberculosis'' alkyl hydroperoxide reductase E (MtAhpE) as model (Pedre et al, 2016). The mutational effects of key residues in its environment are located in the active site. These amino acids create an environment favorising the reaction with peroxides.
 Peroxiredoxins are peroxidases which catalyze the reduction of peroxides (organic peroxide H2O2 or organic hydroperoxides).</div>
@@ Line 22: / Line 22: @@
 According to PDB code 5C04, the structure of the protein has been characterized thanks to crystallography (X-Ray diffraction). The scientists obtained a resolution of 1.45 Å, a R-value free of 0.198 and a R-value work of 0.166. The structure of the 5C04 protein has in total 2 chains (A and B) represented by one sequence-unique entity (one polymer) of L-type polypeptide. Its length is 153 residues. Its secondary structure shows that 27% of alpha helix are composed by six helix for a total of 42 residues; and 27% of beta sheet are composed by 11 strands for also a total of 42 residues.
 [[Image:sequence.png]]
-''Sequence of the 5C04 protein''
+                              ''Sequence of the 5C04 protein''
-[[Image:sequence view chain.png]]
+[[Image:seq2.png]]
-''Sequence view chain''
+                               ''Sequence view chain''
 == Catalytic site ==