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User:Adam Meade/Sandbox 1: Difference between revisions

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=Function of Irr=
=Function of Irr=
Irr behaves differently than other regulatory proteins.  It functions as coordinating the heme biosynthetic pathway, which ends with the insertion of Fe<sup>2+</sup> into a protoporphyrin ring to produce protoheme.  It also controls the pathway by monitoring iron availability to prevent the accumulation of toxic porphyrin precursors under iron limitation, as when iron is limiting, heme cannot be produced.  <ref>Small, S. K., S. Puri, and M. R. O’Brian. 2009. <u>Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other alpha-proteobacteria</u>.  Biometals 22:89-97.</ref>
Irr behaves differently than other regulatory proteins.  To prevent the accumulation of toxic porphyrin precursors under iron limitation, as when iron is limiting, heme cannot be produced.  <ref>Small, S. K., S. Puri, and M. R. O’Brian. 2009. <u>Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other alpha-proteobacteria</u>.  Biometals 22:89-97.</ref>


Irr accumulates in cells under iron limitation, with very low levels of Irr being present in iron-replete cells.  This is a distinction when compared to other Fur family proteins because it functions in the absence of the regulatory metal, whereas the other members require direct metal-binding for the protein to be activated.  <ref>Small, S. K., S. Puri, and M. R. O’Brian. 2009. <u>Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other alpha-proteobacteria</u>.  Biometals 22:89-97.</ref>
Irr accumulates in cells under iron limitation, with very low levels of Irr being present in iron-replete cells.  This is a distinction when compared to other Fur family proteins because it functions in the absence of the regulatory metal, whereas the other members require direct metal-binding for the protein to be activated.  <ref>Small, S. K., S. Puri, and M. R. O’Brian. 2009. <u>Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other alpha-proteobacteria</u>.  Biometals 22:89-97.</ref>
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=Structure of the Proposed Irr Protein=
=Structure of the Proposed Irr Protein=
<applet load='Irr.pdb' size='300' color='black' frame='true' align='right' caption='3D Image of proposed Irr protein'/>
<applet load='Irr.pdb' size='300' color='black' frame='true' align='right' caption='3D Image of proposed Irr protein'/>


<scene name='User:Adam_Meade/Sandbox_1/Secondary_structure_-_irr/1'>Secondary Structure</scene>
<scene name='User:Adam_Meade/Sandbox_1/Secondary_structure_-_irr/1'>Secondary Structure</scene>


<scene name='User:Adam_Meade/Sandbox_1/Polar_regions/1'>Polar/Hydrophobic regions</scene>
<scene name='User:Adam_Meade/Sandbox_1/Polar_regions/2'>Polar/Hydrophobic Regions</scene>
 
<scene name='User:Adam_Meade/Sandbox_1/N_to_c_rainbow/1'>Amino terminus to carboxy terminus</scene>
 
{{Template:ColorKey_Amino2CarboxyRainbow}}
 


The amino acid sequence used to derive the structure shown is as follows:
The amino acid sequence used to derive the structure shown is as follows:
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