Bacteriocin: Colicin-N
Accession: BAC132
Classification
Class: Unclassified
Genetics
Gene: cna
Producer and target organisms
Producer Organism: Escherichia coli [Gram-negative]
Taxonomy: BacteriaProteobacteria
Gammaproteobacteria
Enterobacteriales
Enterobacteriaceae
Escherichia
Target organismsEnterobacteriaceae
Description
The ion-channel forming colicins A, B, E1, Ia, Ib and N all kill bacterial cells selectively by co-opting bacterial active-transport pathways and forming voltage-gated ion conducting channels across the plasma membrane of the target bacterium. The crystal structure of colicin Ia reveals a molecule 210 A long with three distinct functional domains arranged along a backbone of two extraordinarily long alpha-helices. A central domain at the bend of the hairpin-like structure mediates specific recognition and binding to an outer-membrane receptor. A second domain mediates translocation across the outer membrane via the TonB transport pathway; the TonB-box recognition element of colicin Ia is on one side of three 80 A-long helices arranged as a helical sheet. A third domain is made up of 10 alpha-helices which form a voltage-activated and voltage-gated ion conducting channel across the plasma membrane of the target cell. The two 160 A-long alpha-helices that link the receptor-binding domain to the other domains enable the colicin Ia molecule to span the periplasmic space and contact both the outer and plasma membranes simultaneously during function.
Uniprot and PDB links
UniProt Entry: P08083
PDB Entry1A87 resolved by X-ray
NUCLEOTIDE SEQUENCE [GENOMIC DNA].STRAIN=K12;
MEDLINE=88201670;PubMed=2834623;
Pugsley A.P.
"Nucleotide sequencing of the structural gene for colicin N revealshomology between the catalytic, C-terminal domains of colicins A andN.", Mol. Microbiol. 1:317-325(1987).
MEDLINE=88201670;PubMed=2834623;
Pugsley A.P.
"Nucleotide sequencing of the structural gene for colicin N revealshomology between the catalytic, C-terminal domains of colicins A andN.", Mol. Microbiol. 1:317-325(1987).
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 372-387.STRAIN=K12;
MEDLINE=88174431;PubMed=3280946;DOI=10.1007/BF00330613
Pugsley A.P.
"The immunity and lysis genes of ColN plasmid pCHAP4.", Mol. Gen. Genet. 211:335-341(1988).
MEDLINE=88174431;PubMed=3280946;DOI=10.1007/BF00330613
Pugsley A.P.
"The immunity and lysis genes of ColN plasmid pCHAP4.", Mol. Gen. Genet. 211:335-341(1988).
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 91-387.
MEDLINE=98362590;PubMed=9687368;DOI=10.1016/S0969-2126(98)00088-4
Vetter I.R., Parker M.W., Tucker A.D., Lakey J.H., Pattus F., Tsernoglou D.
"Crystal structure of a colicin N fragment suggests a model fortoxicity.", Structure 6:863-874(1998).
MEDLINE=98362590;PubMed=9687368;DOI=10.1016/S0969-2126(98)00088-4
Vetter I.R., Parker M.W., Tucker A.D., Lakey J.H., Pattus F., Tsernoglou D.
"Crystal structure of a colicin N fragment suggests a model fortoxicity.", Structure 6:863-874(1998).
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Gene structure
Gene id | Name | Description | Location |
BACGene593 | colicin N (AA 1 - 387) | 616..1779 |
Protein sequence
........10 ........20 ........30 ........40 ........50 ........60 ........70 ........80 | | | | | | | | MGSNGADNAH NNAFGGGKNP GIGNTSGAGS NGSASSNRGN SNGWSWSNKP HKNDGFHSDG SYHITFHGDN NSKPKPGGNS GNRGNNGDGA SAKVGEITIT PDNSKPGRYI SSNPEYSLLA KLIDAESIKG TEVYTFHTRK GQYVKVTVPD SNIDKMRVDY VNWKGPKYNN KLVKRFVSQF LLFRKEEKEK NEKEALLKAS ELVSGMGDKL GEYLGVKYKN VAKEVANDIK NFHGRNIRSY NEAMASLNKV LANPK |
3D Structure
Protein sequence annotations
Feature | Position(s) | Length | Description |
CHAIN | 1↔387 | 387 | Colicin-N. Feature identifier = PRO_0000218674. |
TRANSMEM | 325↔345 | 21 | Helical; (Potential). |
TRANSMEM | 350↔370 | 21 | Helical; (Potential). |
COMPBIAS | 1↔49 | 49 | Gly-rich. |
STRAND | 97↔101 | 5 | |
STRAND | 108↔112 | 5 | |
HELIX | 114↔116 | 3 | |
TURN | 117↔119 | 3 | |
STRAND | 121↔128 | 8 | |
STRAND | 131↔137 | 7 | |
STRAND | 143↔148 | 6 | |
HELIX | 149↔151 | 3 | |
HELIX | 153↔155 | 3 | |
STRAND | 157↔162 | 6 | |
HELIX | 170↔214 | 45 | |
HELIX | 216↔230 | 15 | |
HELIX | 234↔236 | 3 | |
HELIX | 240↔251 | 12 | |
HELIX | 260↔271 | 12 | |
HELIX | 275↔283 | 9 | |
HELIX | 287↔289 | 3 | |
HELIX | 294↔309 | 16 | |
HELIX | 315↔326 | 12 | |
HELIX | 331↔343 | 13 | |
HELIX | 352↔370 | 19 | |
HELIX | 372↔385 | 14 |
Composition
Hydrophobicity
Composition
Formula | C1844
H2928
N528
O564
S7 |
Absent amino acids | C |
Common amino acids | GNKS |
Mass (Da) | 41767.66 |
Net charge | +23 |
Isoelectric point | 10.22 |
Basic residues | 58 |
Acidic residues | 35 |
Hydrophobic residues | 126 |
Polar residues | 146 |
Aliphatic residues | 37 |
Tiny residues | 72 |
Boman Index | -633.68 |
Hydropathy Index | -0.46 |
Aliphatic Index | 79.87 |
Instability Index | 17.92 (stable) |
Half Life |
Mammalian : 30 hour Yeast : >20 hour E. coli : >10 hour |
Extinction Coefficient | 50880 M-1 cm-1 |
Absorbance 280nm | 131.81 |
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