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. | + | 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> |
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== Disease == | == Disease == | ||
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== 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.
