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'>
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  {{STRUCTURE_2hdi|  PDB=2hdi | SIZE=400| SCENE= |right|CAPTION=E. coli colicin I receptor (grey) complexed with colicin Ia receptor-binding domain (green) and lauryl dimethylamine oxide, [[2hdi]] }}


'''Colicin I receptor''' (Cir) is an E. coli outer membrane protein which binds [[Colicin|colicin]] Ia.  Upon binding it changes its conformation enabling the colicin to insert into the inner membrane forming a voltage-dependent ion channel resulting in killing the bacteria.
== Function ==


{{TOC limit|limit=2}}
'''Colicin I receptor''' (Cir) is a TonB-dependent transporter of E. coli outer membrane transports Fe+3 bound to catecholates.  Cir is used by [[Colicin|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 highlights ==
Cir contains an N-terminal <scene name='46/466463/Cv/2'>plug domain</scene> inserted inside a <scene name='46/466463/Cv/5'>22-stranded transmembrane β barrel</scene>.  The <scene name='46/466463/Cv/6'>colicin Ia R domain</scene> interacts with Cir plug domain.<ref>PMID:17464289</ref>
__NOTOC__
</StructureSection>
== 3D Structures of Colicin I receptor ==
== 3D Structures of Colicin I receptor ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}


[[2hdf]] – EcCir – ''Escherichia coli''<br />
[[2hdf]] – EcCir – ''Escherichia coli''<br />
[[2hdi]] – EcCir + colicin Ia receptor-binding domain
[[2hdi]] – EcCir + colicin Ia receptor-binding domain
== References ==
<references/>


[[Category:Topic Page]]
[[Category:Topic Page]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky