View bacteriocin : Colicin-E1

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Accession BAC130
Name Colicin-E1
Related Entries Colicin-V (Microcin-V)Colicin-10Colicin-NColicin-MColicin-Ia

Colicin-Ib
Gene cea
Class Unclassified
Producer Organism Escherichia coli [Gram-negative]
Taxonomy BacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Target organisms Enterobacteriaceae
Swiss-Prot Entry P02978
PDB Entry 2I88 resolved by X-ray
Other databases EMBL J01563EMBL U15633PIR A93913TCDB 1.C.1.2.2GO GO:0016021

GO GO:0005886GO GO:0005102GO GO:0019835GO GO:0050829InterPro IPR000293

Gene3D G3DSA:1.10.490.30Pfam PF01024PRINTS 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 
          |          |          |          |          |          |          |          | 
 METAVAYYKD GVPYDDKGQV IITLLNGTPD GSGSGGGGGK GGSKSESSAA IHATAKWSTA QLKKTQAEQA ARAKAAAEAQ
 AKAKANRDAL TQRLKDIVNE ALRHNASRTP SATELAHANN AAMQAEDERL RLAKAEEKAR KEAEAAEKAF QEAEQRRKEI
 EREKAETERQ LKLAEAEEKR LAALSEEAKA VEIAQKKLSA AQSEVVKMDG EIKTLNSRLS SSIHARDAEM KTLAGKRNEL
 AQASAKYKEL DELVK
Structure
Composition
Formula C2504 H4101 N731 O790 S6
Absent amino acids
Common amino acids A
Mass (Da) 57306.93
Net charge +21
Isoelectric point 9.91
Basic residues 94
Acidic residues 73
Hydrophobic residues 192
Polar residues 127
Aliphatic residues 36
Tiny residues 82
Boman Index -1117.77
Hydropathy Index -0.59
Aliphatic Index 83.01
Instability Index 29.08 (stable)
Half Life Mammalian : 30 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 41370 M-1 cm-1
Absorbance 280nm 79.4
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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