1col

REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTIONREFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION

Structural highlights

1col is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CEA_ECOLX] This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.^[1] Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The E1 subgroup (E1, A, B, IA, IB, K and N) of anti-bacterial toxins called colicins is known to form voltage-dependent channels in lipid bilayers. The crystal structure of the pore-forming domain of colicin A from Escherichia coli has been refined to the diffraction limit of the crystals at 2.4 A resolution by means of molecular dynamics and restrained least-squares methods to a conventional R-factor of 0.18 for all data between 6.0 and 2.4 A resolution. The polypeptide chain of 204 amino acid residues consists of ten alpha-helices organized in a three-layer structure. The helices range in length from 9 to 23 residues with an average length of 125 residues. The packing arrangement of the helices has been analysed; the packing is different from that observed in four-helix bundle proteins. The sites of 83 water molecules have been located and refined. Analysis of the structure provides insights into the mechanism of formation of a voltage-gated channel by the protein. Although it is proposed that substantial tertiary structural changes occur during membrane insertion, the secondary structural elements remain conserved. This idea has been proposed recently for a number of other protein-membrane events and thus may have more general applicability.

Refined structure of the pore-forming domain of colicin A at 2.4 A resolution.,Parker MW, Postma JP, Pattus F, Tucker AD, Tsernoglou D J Mol Biol. 1992 Apr 5;224(3):639-57. PMID:1373773^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Baty D, Knibiehler M, Verheij H, Pattus F, Shire D, Bernadac A, Lazdunski C. Site-directed mutagenesis of the COOH-terminal region of colicin A: effect on secretion and voltage-dependent channel activity. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1152-6. PMID:2434951
↑ Baty D, Knibiehler M, Verheij H, Pattus F, Shire D, Bernadac A, Lazdunski C. Site-directed mutagenesis of the COOH-terminal region of colicin A: effect on secretion and voltage-dependent channel activity. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1152-6. PMID:2434951
↑ Parker MW, Postma JP, Pattus F, Tucker AD, Tsernoglou D. Refined structure of the pore-forming domain of colicin A at 2.4 A resolution. J Mol Biol. 1992 Apr 5;224(3):639-57. PMID:1373773

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Baty D, Knibiehler M, Verheij H, Pattus F, Shire D, Bernadac A, Lazdunski C. Site-directed mutagenesis of the COOH-terminal region of colicin A: effect on secretion and voltage-dependent channel activity. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1152-6. PMID:2434951

[2] Baty D, Knibiehler M, Verheij H, Pattus F, Shire D, Bernadac A, Lazdunski C. Site-directed mutagenesis of the COOH-terminal region of colicin A: effect on secretion and voltage-dependent channel activity. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1152-6. PMID:2434951

[3] Parker MW, Postma JP, Pattus F, Tucker AD, Tsernoglou D. Refined structure of the pore-forming domain of colicin A at 2.4 A resolution. J Mol Biol. 1992 Apr 5;224(3):639-57. PMID:1373773

[1]

[2]

[3]