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<StructureSection load='1cii' size='340' side='right' caption='Crystal structure of Colicin Ia, the first colicin to be identified, [[1cii]].  ' scene=''>
<StructureSection load='1cii' size='340' side='right' caption='Crystal structure of Colicin Ia, the first colicin to be identified, [[1cii]].  ' scene=''>
__TOC__
==Function==
'''Colicins''' are a type of bacteriocin - peptide and protein antibiotics released by bacteria to kill other bacteria of the same species, in order to provide a competitive advantage for nutrient acquisition <ref> PMID: 16166536 </ref>. Bacteriocins are named after their species of origin; colicins are so-called because they are produced by <i>E. Coli</i><ref>PMID: 17347522 </ref>. Because of their narrow killing spectrum which focuses primarily on the species which has made the peptide (or occasionally closely related species<ref> PMID: 12423779 </ref>), bacteriocins are important in microbial biodiversity and the stable co-existence of the bacterial populations<ref> PMID: 11792831 </ref><ref>PMID: 12110887 </ref>.
'''Colicins''' are a type of bacteriocin - peptide and protein antibiotics released by bacteria to kill other bacteria of the same species, in order to provide a competitive advantage for nutrient acquisition <ref> PMID: 16166536 </ref>. Bacteriocins are named after their species of origin; colicins are so-called because they are produced by <i>E. Coli</i><ref>PMID: 17347522 </ref>. Because of their narrow killing spectrum which focuses primarily on the species which has made the peptide (or occasionally closely related species<ref> PMID: 12423779 </ref>), bacteriocins are important in microbial biodiversity and the stable co-existence of the bacterial populations<ref> PMID: 11792831 </ref><ref>PMID: 12110887 </ref>.


Colicin peptides are plasmid-encoded. The peptide is released by the cell into the area surrounding it, and then parasitises proteins present in the host cell membrane to translocate across into the host cell. Many protein-protein interactions are involved in the cell entry, and the main system is involved in the grouping of colicins into two families: Group A colicins use the [[Tol]] system to enter the host cell, and Group B use the [[Ton]] system. Once inside the host cell, the cell killing follows 1st order kinetics - ie one molecule is theoretically sufficient to kill the cell<ref> PMID: 7577966 </ref>.
Colicin peptides are plasmid-encoded. The peptide is released by the cell into the area surrounding it, and then parasitises proteins present in the host cell membrane to translocate across into the host cell. Many protein-protein interactions are involved in the cell entry, and the main system is involved in the grouping of colicins into two families: Group A colicins use the [[Tol]] system to enter the host cell, and Group B use the [[Ton]] system. Once inside the host cell, the cell killing follows 1st order kinetics - ie one molecule is theoretically sufficient to kill the cell<ref> PMID: 7577966 </ref>.
*'''Colicin-A''' see [[Colicin-A]]
*'''Colicin-B''' forms small, ion-permeable channels.  It inhibits the transport of Pro and enhances the transport of methylglucoside<ref> PMID:2419320 </ref>.
*'''Colicin-D''' cleaves the anticodon loop of tRNAArg<ref> PMID:15014439 </ref>
*'''Colicin-E1''' binds to TolC and plug channels of Gram-negative bacteria<ref> PMID:35199644 </ref>
*'''Colicin-E2''' and '''Colicin-E9''' bind to BtuB and cleaves the target DNA<ref> PMID:17416663 </ref>, <ref> PMID:15995205 </ref>
*'''Colicin-E3''' cleaves the ribosome A site<ref> PMID:11741540 </ref>
*'''Colicin-E5''' cleaves tRNA which contain the nucleotide queuosine<ref> PMID:16060658 </ref>
*'''Colicin-E7''' binds to immunity protein 7<ref> PMID:10368275 </ref>
*'''Colicin-Ia''' see [[Colicin-Ia]]
*'''Colicin-M''' cleaves peptidoglycans by hydrolysing their phosphoester bonds<ref> PMID:23176510 </ref>


The structure of all colicins, of which over 20 have been identified, follows a 3 domain design:
The structure of all colicins, of which over 20 have been identified, follows a 3 domain design:
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*[[Translocation domain]]<br />
*[[Translocation domain]]<br />
*[[H-N-H motif]]<br />
*[[H-N-H motif]]<br />
*[[Colicin A]]<br />
*[[16s rRNase activity]]<br />
*[[16s rRNase activity]]<br />
*[[Colicin Ia]].
*[[Cloacin DF13]].
*[[Colicin Immunity Protein]]


==Synthesis, Production and Release==
==Synthesis, Production and Release==
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Table taken from <ref>PMID: 21060316 </ref> except where indicated.
Table taken from <ref>PMID: 21060316 </ref> except where indicated.
==SEE ALSO==
 
[[Colicin Immunity Protein]]
<StructureSection
==3D structure of Colicin==
==3D structure of Colicin==
[[Colicin 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*Colicin-A
 
**[[3iax]], [[3qdr]] – CfColA translocation domain + EcTolB – ''Citrobacter freundii''<br />
**[[1col]] – EcColA pore-forming domain
 
*Colicin-B
 
**[[1rh1]] - EcColB
 
*Colicin-D
 
**[[1tfk]], [[1tfo]], [[1v74]] - EcColD catalytic domain + EcColD immunity protein<br />
 
*Colicin-E1
 
**[[2i88]] – EcColE1 channel-forming domain
 
*Colicin-E2
 
**[[2ysu]] – EcColE2 receptor-binding domain + BtuB<br />
**[[3u43]] – EcColE2 nuclease domain + EcColE2 immunity protein
 
*Colicin-E3
 
**[[4v5k]] – EcColE3 cytotoxic domain (mutant) + Tt30S ribosome – ''Thermos thermophilus''<br />
**[[2zld]] - EcColE3 cytotoxic domain + outer membrane protein F<br />
**[[1jch]] – EcColE3 + EcColE3 immunity protein<br />
**[[2b5u]] – EcColE3 (mutant) + EcColE3 immunity protein<br />
**[[1e44]] – EcColE3 nuclease domain + EcColE3 immunity protein<br />
**[[1ujw]] – EcColE3 receptor-binding domain + BtuB
 
*Colicin-E5
 
**[[2djh]], [[3ao9]] – EcColE5 C-terminal domain<br />
**[[3vj7]] - EcColE5 C-terminal domain (mutant)<br />
**[[2a8k]] – EcColE5 catalytic domain<br />
**[[2dfx]] – EcColE5 C-terminal domain + EcColE5 immunity protein<br />
**[[2fhz]] – EcColE5 residues 74-180 + EcColE5 immunity protein<br />
 
*Colicin-E7
 
**[[1unk]] - EcColE7<br />
**[[2axc]] - EcColE7 translocation domain<br />
**[[1m08]], [[3zfk]] - EcColE7 nuclease domain<br />
**[[3fbd]], [[1zns]], [[2ivh]] – EcColE7 (mutant) + DNA<br />
**[[1pt3]] - EcColE7 nuclease domain + DNA<br />
**[[1mz8]], [[7cei]] - EcColE7 nuclease domain + EcColE7 immunity protein<br />
**[[3gjn]] - EcColE7 nuclease domain + EcColE9 immunity protein (mutant) <br />
**[[3gkl]] - EcColE7 nuclease domain (mutant) + EcColE9 immunity protein (mutant) <br />
**[[2jaz]], [[2jb0]], [[2jbg]], [[1znv]] - EcColE7 nuclease domain (mutant) + EcColE7 immunity protein<br />
**[[2erh]], [[1ujz]] - EcColE7 (mutant) + EcColE7 immunity protein (mutant)
 
*Colicin-E9
 
**[[1fsj]] - EcColE9 DNase domain<br />
**[[1v13]] - EcColE9 DNase domain (mutant) <br />
**[[1v14]], [[1v15]] - EcColE9 DNase domain (mutant) + DNA<br />
**[[2wpt]] – EcColE9 (mutant) + EcColE2 immunity protein<br />
**[[2k5x]], [[1emv]], [[1bxi]] – EcColE9 DNase domain + EcColE9 immunity protein<br />
**[[2vln]], [[2vlo]], [[2vlp]], [[2vlq]] - EcColE9 DNase domain (mutant) + EcColE9 immunity protein<br />
**[[2gze]], [[2gzg]], [[2gzi]], [[2gzj]], [[2gzf]], [[2gyk]], [[1fr2]] - EcColE9 DNase domain + EcColE9 immunity protein (mutant)<br />
**[[2ivz]] - EcColE9 T domain + TolB<br />
**[[3o0e]] - EcColE9 fragment + outer membrane porin 1A
 
*Colicin-Ia
 
**[[1cii]] - EcColIa<br />
**[[2hdi]] – EcColIA R domain + ColI receptor
 
*Colicin-M
 
**[[2xmx]], [[3da3]], [[3da4]] – EcColM<br />
**[[2xtq]], [[2xtr]] – EcColM (mutant)
 
*Colicin-N
 
**[[1a87]] – EcColN receptor-binding domain
 
*Colicin-S4


**[[3few]] – EcColS4
}}
==References==
==References==
<references/>
<references/>


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

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

Gemma McGoldrick, Michal Harel, Alexander Berchansky, Jaime Prilusky
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