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 ==
 
'''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>


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</StructureSection>
== 3D Structures of Colicin I receptor ==
== 3D Structures of Colicin I receptor ==


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[[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]]

Latest revision as of 09:30, 18 February 2019


Function

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 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 inserted inside a . The interacts with Cir plug domain.[1]


E. coli colicin I receptor (cyan) complexed with colicin Ia receptor-binding domain (green) and lauryl dimethylamine oxide (PDB entry 2hdi)

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3D Structures of Colicin I receptor3D Structures of Colicin I receptor

Updated on 18-February-2019

2hdf – EcCir – Escherichia coli
2hdi – EcCir + colicin Ia receptor-binding domain

ReferencesReferences

  1. Buchanan SK, Lukacik P, Grizot S, Ghirlando R, Ali MM, Barnard TJ, Jakes KS, Kienker PK, Esser L. Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import. EMBO J. 2007 May 16;26(10):2594-604. Epub 2007 Apr 26. PMID:17464289

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Michal Harel, Alexander Berchansky