Mutant immunity protein 9 (variant R12-13)

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<StructureSection load='3gkl' size='350' frame='true' align='right' scene='' caption='Colicin-E9 immunity protein fragment (grey and green) complex with colicin-E7 (yellow and pink) (PDB code [[3gkl]])' >
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<StructureSection load='3gkl' size='350' scene='' caption='Colicin-E9 immunity protein fragment (grey and green) complex with colicin-E7 (yellow and pink) (PDB code [[3gkl]])' >
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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.

Current revision

Colicin-E9 immunity protein fragment (grey and green) complex with colicin-E7 (yellow and pink) (PDB code 3gkl)

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See also

About this Structure

3GJN is a 4 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Levin KB, Dym O, Albeck S, Magdassi S, Keeble AH, Kleanthous C, Tawfik DS. Following evolutionary paths to protein-protein interactions with high affinity and selectivity. Nat Struct Mol Biol. 2009 Oct;16(10):1049-55. Epub 2009 Sep 13. PMID:19749752 doi:10.1038/nsmb.1670

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Alexander Berchansky, Michal Harel, Jaime Prilusky

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