Colicin I receptor
From Proteopedia
(Difference between revisions)
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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. | ||
| - | + | <StructureSection load='2hdi' size='350' side='right' caption='E. coli colicin I receptor (grey) complexed with colicin Ia receptor-binding domain (green) and lauryl dimethylamine oxide (PDB entry [[2hdi]])' scene=''> | |
| + | == Function == | ||
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| + | '''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. | ||
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| + | == Structural highlights == | ||
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| + | 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.<ref>PMID:17464289</ref> | ||
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| + | __NOTOC__ | ||
| + | </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 | ||
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| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:23, 13 December 2015
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3D Structures of Colicin I receptor
Updated on 13-December-2015
2hdf – EcCir – Escherichia coli
2hdi – EcCir + colicin Ia receptor-binding domain
