Sandbox Reserved 654: Difference between revisions

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'''Catalytic Domain'''
'''Catalytic Domain'''
 
<scene name='Sandbox_Reserved_654/Four-helix/1'>TextToBeDisplayed</scene>
The <scene name='Sandbox_Reserved_642/Catalytic_domain/1'>catalytic domain</scene> of phenylalanine hydroxylase includes resides 143-410.  This region has a basket-like arrangement consisting of 13 alpha-helices and 8 beta-strands. This region of the protein also includes the active site.  The active site of PheOH can be found in the center of the catalytic domain and is characterized by a 13 Angstroms deep and 10 Angstroms wide hydrophobic pocket. Lining the active site are 3 glutamates, 2 histadines and 1 tyrosine residue along with hydrophobic residues for a total of 34 amino acids. Covering the entrance of the active site is a short loop consisting or residues 378-381.   
The <scene name='Sandbox_Reserved_642/Catalytic_domain/1'>catalytic domain</scene> of phenylalanine hydroxylase includes resides 143-410.  This region has a basket-like arrangement consisting of 13 alpha-helices and 8 beta-strands. This region of the protein also includes the active site.  The active site of PheOH can be found in the center of the catalytic domain and is characterized by a 13 Angstroms deep and 10 Angstroms wide hydrophobic pocket. Lining the active site are 3 glutamates, 2 histadines and 1 tyrosine residue along with hydrophobic residues for a total of 34 amino acids. Covering the entrance of the active site is a short loop consisting or residues 378-381.   
The center of each catalytic domain consists of an iron ion which is vital to the enzyme activity.  The iron atom binds in the active site to  <scene name='Sandbox_Reserved_642/Iron_binding/2'>histadine residues 285 and 290, 1 oxygen atom in glutamate 330</scene>. Histadine 285 and 290 were found to be required for the binding of iron through site directed mutagenisis studies.  The iron ions are coordinated to three water molecules and arrange in an octahedral geometry.  The active site also binds the  
The center of each catalytic domain consists of an iron ion which is vital to the enzyme activity.  The iron atom binds in the active site to  <scene name='Sandbox_Reserved_642/Iron_binding/2'>histadine residues 285 and 290, 1 oxygen atom in glutamate 330</scene>. Histadine 285 and 290 were found to be required for the binding of iron through site directed mutagenisis studies.  The iron ions are coordinated to three water molecules and arrange in an octahedral geometry.  The active site also binds the