| General information | | DisProt: | DP00461 | | Name: | Colicin-N | | Synonym(s): | CEAN_ECOLX
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | P08083 | | UniGene: | | | SwissProt: | CEAN_ECOLX | | TrEMBL: | | | NCBI (GI): | 116070 | | Source organism: | Escherichia coli | | Sequence length: | 387 | | Percent disordered: | 8% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MGSNGADNAH NNAFGGGKNP GIGNTSGAGS NGSASSNRGN SNGWSWSNKP HKNDGFHSDG - 60
SYHITFHGDN NSKPKPGGNS GNRGNNGDGA SAKVGEITIT PDNSKPGRYI SSNPEYSLLA - 120
KLIDAESIKG TEVYTFHTRK GQYVKVTVPD SNIDKMRVDY VNWKGPKYNN KLVKRFVSQF - 180
LLFRKEEKEK NEKEALLKAS ELVSGMGDKL GEYLGVKYKN VAKEVANDIK NFHGRNIRSY - 240
NEAMASLNKV LANPKMKVNK SDKDAIVNAW KQVNAKDMAN KIGNLGKAFK VADLAIKVEK - 300
IREKSIEGYN TGNWGPLLLE VESWIIGGVV AGVAISLFGA VLSFLPISGL AVTALGVIGI - 360
MTISYLSSFI DANRVSNINN IISSVIR
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| Functional narrative |
This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.
Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Translocation domain | | Location: | 40 - 69 | | Length: | 30 | | Region sequence: |
NSNGWSWSNKPHKNDGFHSDGSYHITFHGD | | Modification type: | Fragment
Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular recognition effectors
Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7; ammonium phosphate 10 mM)
- Circular dichroism (CD) spectroscopy, near-UV (pH: 7; ammonium phosphate 10 mM)
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7.4; NaCl 300 mM; phosphate 20 mM; TFE 75 %)
- X-ray crystallography (298 K; pH: 7; ammonium sulphate (w/v) 40 %; PEG 6000 (0-5%); phosphate 50 mM)
- Nuclear magnetic resonance (NMR) (pH: 5; acetate buffer)
| References:
- Anderluh G, Gokce I, Lakey JH. "A natively unfolded toxin domain uses its receptor as a folding template." J Biol Chem. 2004; 279(21): 22002-9. PubMed: 15004032
- Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. "Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA." J Biol Chem. 2003; 278(24): 21860-8. PubMed: 12679333
- Gokce I, Raggett EM, Hong Q, Virden R, Cooper A, Lakey JH. "The TolA-recognition site of colicin N. ITC, SPR and stopped-flow fluorescence define a crucial 27-residue segment." J Mol Biol. 2000; 304(4): 621-32. PubMed: 11099384
- Hecht O, Ridley H, Boetzel R, Lewin A, Cull N, Chalton DA, Lakey JH, Moore GR. "Self-recognition by an intrinsically disordered protein." FEBS Lett. 2008; 582(17): 2673-7. PubMed: 18573254
- Raggett EM, Bainbridge G, Evans LJ, Cooper A, Lakey JH. "Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: a biophysical approach." Mol Microbiol. 1998; 28(6): 1335-43. PubMed: 9680221
- Vetter IR, Parker MW, Tucker AD, Lakey JH, Pattus F, Tsernoglou D. "Crystal structure of a colicin N fragment suggests a model for toxicity." Structure. 1998; 6(7): 863-74. PubMed: 9687368
- Zakharov SD, Eroukova VY, Rokitskaya TI, Zhalnina MV, Sharma O, Loll PJ, Zgurskaya HI, Antonenko YN, Cramer WA. "Colicin occlusion of OmpF and TolC channels: outer membrane translocons for colicin import." Biophys J. 2004; 87(6): 3901-11. PubMed: 15465872
| Comments:The translocation domain of this protein is needed for the importing of the protein across the outer membrane. It binds to the third domain of TolA protein, and probably also binds to the OmpF protein. Residues 1-40 may be removed without abolishing toxicity. Residues 40-67 are essential for TolA binding.
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