Colicin I receptor

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 plug domain inserted inside a 22-stranded transmembrane β barrel. The colicin Ia R domain interacts with Cir plug domain.^[1]

E. coli colicin I receptor (grey) 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 13-December-2015

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

ReferencesReferences

↑ 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

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

Michal Harel, Alexander Berchansky

[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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