Colicin I receptor: Difference between revisions
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<StructureSection load='2hdi' size='350' side='right' caption='E. coli colicin I receptor (cyan) complexed with colicin Ia receptor-binding domain (green) and lauryl dimethylamine oxide (PDB entry [[2hdi]])' scene='46/466463/Cv/1'> | |||
<StructureSection load='2hdi' size='350' side='right' caption='E. coli colicin I receptor ( | |||
== Function == | == Function == |
Revision as of 12:43, 20 December 2015
FunctionColicin I receptor (Cir) is a TonB-dependent transporter of E. coli outer membrane transports Fe+3 bound to catecholates. Cir is used by colicin Ia to penetrate the cell. Upon binding to colicin Ia Cir changes its conformation enabling the colicin to insert into the inner membrane forming a voltage-dependent ion channel resulting in killing the bacteria. Structural highlightsCir contains an N-terminal plug domain inserted inside a 22-stranded transmembrane β barrel. The colicin Ia R domain interacts with Cir plug domain.[1]
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3D Structures of Colicin I receptor3D Structures of Colicin I receptor
Updated on 20-December-2015
2hdf – EcCir – Escherichia coli
2hdi – EcCir + colicin Ia receptor-binding domain