Colicin Immunity Protein: Difference between revisions

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[[Image:1ayi.png|left|200px|thumb|Crystal Structure of Colicin immunity protein, [[1ayi]]]]
<StructureSection load='3gkl' size='500' frame='true' align='right' scene='3gkl/Al/1' >
{{STRUCTURE_1ayi|  PDB=1ayi  | SIZE=400| SCENE=Colicin_Immunity_Protein/Colicin_immunity_protein/1 |right|CAPTION=Colicin-E7 immunity protein, [[1ayi]] }}
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
'''Immunity proteins''' against [[Colicin]]s (EcCIP) are produced by ''E. coli'' alongside the relevant colicin protein (EcCol) to protect the cell from the cytotoxic domain of the colicin. Usually this involves binding to and blocking the active site of the domain, to prevent it from targeting the cells own mechanisms.  
'''Immunity proteins''' against [[Colicin]]s (EcCIP) are produced by ''E. coli'' alongside the relevant colicin protein (EcCol) to protect the cell from the cytotoxic domain of the colicin. Usually this involves binding to and blocking the active site of the domain, to prevent it from targeting the cells own mechanisms.  


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{{Clear}}
{{Clear}}
==Directed evolution and Colicin7/Immunity-proteins complexes<ref>PMID:19749752</ref>==
==Directed evolution and Colicin7/Immunity-proteins complexes<ref>PMID:19749752</ref>==
<StructureSection load='3gkl' size='500' frame='true' align='right' scene='3gkl/Al/1' >
 
Iterative rounds of random mutagenesis and selection of <span style="color:yellow;background-color:black;font-weight:bold;">immunity protein 9 (colored yellow)</span> toward higher affinity for ColE7, and selectivity (against ColE9 inhibition), led to significant increase in affinity and selectivity. Several evolved variants were obtained. The crystal structures of the two final generation <scene name='3gkl/Al/3'>variants</scene> <span style="color:lime;background-color:black;font-weight:bold;">R12-2</span> ('''3gkl'''; T20A, N24D, T27A, S28T, V34D, V37J, E41G, and K57E) and <font color='darkred'><b>R12-13</b></font> ([[3gjn]]; N24D, D25E, T27A, S28T, V34D, V37J, and Y55W) in complex with ColE7 were solved.  
Iterative rounds of random mutagenesis and selection of <span style="color:yellow;background-color:black;font-weight:bold;">immunity protein 9 (colored yellow)</span> toward higher affinity for ColE7, and selectivity (against ColE9 inhibition), led to significant increase in affinity and selectivity. Several evolved variants were obtained. The crystal structures of the two final generation <scene name='3gkl/Al/3'>variants</scene> <span style="color:lime;background-color:black;font-weight:bold;">R12-2</span> ('''3gkl'''; T20A, N24D, T27A, S28T, V34D, V37J, E41G, and K57E) and <font color='darkred'><b>R12-13</b></font> ([[3gjn]]; N24D, D25E, T27A, S28T, V34D, V37J, and Y55W) in complex with ColE7 were solved.