Bacteriocin: Colicin-N

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Bacteriocin: Colicin-N

Accession: BAC132

Classification
Class: Unclassified
Genetics
Gene: cna
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).
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).
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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Gene structure
genome of Colicin-N

Gene idNameDescriptionLocation
BACGene593colicin 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

FeaturePosition(s)LengthDescription
CHAIN1↔387387
Colicin-N.
Feature identifier = PRO_0000218674.
TRANSMEM325↔34521Helical; (Potential).
TRANSMEM350↔37021Helical; (Potential).
COMPBIAS1↔4949Gly-rich.
STRAND97↔1015
STRAND108↔1125
HELIX114↔1163
TURN117↔1193
STRAND121↔1288
STRAND131↔1377
STRAND143↔1486
HELIX149↔1513
HELIX153↔1553
STRAND157↔1626
HELIX170↔21445
HELIX216↔23015
HELIX234↔2363
HELIX240↔25112
HELIX260↔27112
HELIX275↔2839
HELIX287↔2893
HELIX294↔30916
HELIX315↔32612
HELIX331↔34313
HELIX352↔37019
HELIX372↔38514
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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