View bacteriocin : Colicin-10

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Accession BAC131
Name Colicin-10
Related Entries Colicin-V (Microcin-V)Colicin-E1Colicin-NColicin-MColicin-Ia

Colicin-Ib
Gene cta
Class Unclassified
Producer Organism Escherichia coli [Gram-negative]
Taxonomy BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organisms Enterobacteriaceae
Swiss-Prot Entry Q47125
PDB Entry Unknown
Other databases EMBL X82682PIR I41024TCDB 1.C.1.2.3GO GO:0016021GO GO:0005102

GO GO:0019835GO GO:0050829InterPro IPR000293Gene3D G3DSA:1.10.490.30Pfam PF01024

PRINTS PR00280ProDom PD002657PROSITE 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]


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Sequence
 ........10 ........20 ........30 ........40 ........50 ........60 ........70 ........80 
          |          |          |          |          |          |          |          | 
 MDKVTDNSPD VESTESTEGS FPTVGVDTGD TITATLATGT ENVGGGGGAF GGASESSAAI HATAKWSTAQ LKKHQAEQAA
 RAAAAEAALA KAKSQRDALT QRLKDIVNDA LRANAARSPS VTDLAHANNM AMQAEAERLR LAKAEQKARE EAEAAEKALR
 EAERQRDEIA RQQAETAHLL AMAEAAEAEK NRQDSLDEEH RAVEVAEKKL AEAKAELAKA ESDVQSKQAI VSRVAGELEN
 AQKSVDVKVT GFPGW
Composition
Formula C2333 H3753 N657 O759 S6
Absent amino acids C
Common amino acids A
Mass (Da) 53369.26
Net charge -6
Isoelectric point 5.1
Basic residues 74
Acidic residues 80
Hydrophobic residues 187
Polar residues 115
Aliphatic residues 36
Tiny residues 86
Boman Index -971.84
Hydropathy Index -0.49
Aliphatic Index 81.2
Instability Index 20.98 (stable)
Half Life Mammalian : 30 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 47900 M-1 cm-1
Absorbance 280nm 97.96
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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