Sandbox ggc5
From Proteopedia
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== '''Dye-decolorizing Peroxidase YfeX from ''Escherichia Coli''''' == | == '''Dye-decolorizing Peroxidase YfeX from ''Escherichia Coli''''' == | ||
<StructureSection load='5GT2' size='340' side='right' caption='dye-decolorizing peroxidase YfeX from Escherichia coli' scene=''> | <StructureSection load='5GT2' size='340' side='right' caption='dye-decolorizing peroxidase YfeX from Escherichia coli' scene=''> | ||
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== Function == | == Function == | ||
| - | + | YfeX is a dye-decolorizing peroxidase that has a very high specificity for its substrate. This protein belongs to the heme super family known as Dyp and has recently been discovered in bacteria and fungi <ref>Xiuhua Liu, Z. Y. (2017). Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143 and Arg232 play divergent roles toward different substrates. Biochemical and Biophysical Research Communications, 40-44.</ref>. When loaded with heme, the YfeX becomes an effective Dyp and can decolorize alazine red and degrade anthraquinone dye <ref>Xiuhua Liu, Z. Y. (2017). Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143 and Arg232 play divergent roles toward different substrates. Biochemical and Biophysical Research Communications, 40-44.</ref> | |
| + | == Disease == | ||
| + | The dye-decolorizing peroxidase YfeX is present in ''E. Coli'' bacteria and has been thought to be used as a method to obtain the iron necessary for survival from the heme group of its hosts. Research has been done to find the correlation between the two. Although no hard evidence has been obtained, there is still reason to believe there is a connection between the peroxidase and the means for iron acquisition. | ||
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| - | == Disease == | ||
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| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
| - | <scene name='75/752267/Color_by_secondary_structure/1'>secondary structure</scene> | ||
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| - | <scene name='75/752267/Ligands_highlighted/1'>4 ligands</scene> | ||
| - | <scene name='75/752267/Heme_groups/1'>Heme groups</scene> | + | The YfeX Dyp contains four <scene name='75/752267/Heme_groups/1'>Heme groups</scene>. These heme groups are surrounded by <scene name='75/752267/Amino_acids/1'>three amino acid residues</scene> that are conserved across this peroxidase super family. (His 215-purple, Asp 143-blue, Arg 232-yellow) |
| - | + | :*'''His 215''': proximal axial ligand of the heme iron atom | |
| + | :*'''Asp 143 and Arg 232''': Catalytic role varies with divergence of substrate and substrate type | ||
| - | <scene name='75/752267/Sheets_vs_helix/ | + | There are <scene name='75/752267/Sheets_vs_helix/4'>10 α-helices and 8 β-sheets</scene>. The structure of the YfeX monomer shows traits related to the Dyp super family in that the β-strands are anti- parallel. The N and C terminal domains are connected by a twenty amino acid long loop. |
| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
</StructureSection> | </StructureSection> | ||
Current revision
Dye-decolorizing Peroxidase YfeX from Escherichia Coli
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References
- ↑ Xiuhua Liu, Z. Y. (2017). Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143 and Arg232 play divergent roles toward different substrates. Biochemical and Biophysical Research Communications, 40-44.
- ↑ Xiuhua Liu, Z. Y. (2017). Crystal structure and biochemical features of dye-decolorizing peroxidase YfeX from Escherichia coli O157 Asp143 and Arg232 play divergent roles toward different substrates. Biochemical and Biophysical Research Communications, 40-44.
