Colicin: Difference between revisions
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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=''> | |||
__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>. | |||
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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<br>The Receptor binding domain is at the centre of the peptide (R-): Residues <scene name='Colicin/Rdomaincolia/1'>~190 to 451</scene> in ColIa. | <br>The Receptor binding domain is at the centre of the peptide (R-): Residues <scene name='Colicin/Rdomaincolia/1'>~190 to 451</scene> in ColIa. | ||
<br>The C terminus contains the Cytotoxic domain (C-): Residues <scene name='Colicin/Cdomaincolia/1'>452 to 626</scene> in ColIa<ref> PMID: 7543362 </ref>. | <br>The C terminus contains the Cytotoxic domain (C-): Residues <scene name='Colicin/Cdomaincolia/1'>452 to 626</scene> in ColIa<ref> PMID: 7543362 </ref>. | ||
[[Image: Colicin_Domain_structure.png|500px|thumb| The 3 domain structure of all colicins]] | |||
[[ | Some colicins exhibit [[DNase Activity]] and others [[TRNase activity]]. For more details see also <br /> | ||
*[[Pore Formation]]<br /> | |||
*[[Translocation domain]]<br /> | |||
*[[H-N-H motif]]<br /> | |||
*[[16s rRNase activity]]<br /> | |||
*[[Cloacin DF13]]. | |||
*[[Colicin Immunity Protein]] | |||
==Synthesis, Production and Release== | ==Synthesis, Production and Release== | ||
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! Colicin !! Group !! OM Receptor !! Translocation Proteins !! Cytotoxic activity !! Immunity protein | ! Colicin !! Group !! OM Receptor !! Translocation Proteins !! Cytotoxic activity !! Immunity protein | ||
|- | |- | ||
| [[Colicin A]] || A || BtuB || OmpF/[[Tol]]QRAB || Pore-forming || [[ | | [[Colicin A]] || A || BtuB || OmpF/[[Tol]]QRAB || Pore-forming || [[Colicin_Immunity_Protein]]<ref> PMID: 11673448 </ref> | ||
|- | |- | ||
| [[Colicin E1]] || A || BtuB || TolC/TolAQ || Pore-forming || [[ImmE1]]<ref> PMID: 1708384 </ref> | | [[Colicin E1]] || A || BtuB || TolC/TolAQ || Pore-forming || [[ImmE1]]<ref> PMID: 1708384 </ref> | ||
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==3D structure of Colicin== | ==3D structure of Colicin== | ||
[[Colicin 3D structures]] | |||
</StructureSection> | |||
==References== | ==References== |