View bacteriocin : Colicin-N

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Accession BAC132
Name Colicin-N
Related Entries Colicin-V (Microcin-V)Colicin-E1Colicin-10Colicin-MColicin-Ia

Colicin-Ib
Gene cna
Class Unclassified
Producer Organism Escherichia coli [Gram-negative]
Taxonomy BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organisms Enterobacteriaceae
Swiss-Prot Entry P08083
PDB Entry 1A87 resolved by X-ray
Other databases EMBL Y00533EMBL X06933PIR S00867DisProt DP00461TCDB 1.C.1.3.3

GO GO:0016021GO GO:0005886GO GO:0005102GO GO:0019835GO GO:0050829

InterPro IPR000293Gene3D G3DSA:1.10.490.30Pfam PF01024PRINTS PR00280ProDom PD002657

PROSITE PS00276
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.
[Ref. 1] | View abstract | Export citation
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).

[Ref. 2] | View abstract | Export citation
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).

[Ref. 3] | View abstract | Export citation
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).

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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
Structure
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
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).


Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).


Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

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