PMID:10380085
| Citation |
Derouiche, R, Lloubès, R, Sasso, S, Bouteille, H, Oughideni, R, Lazdunski, C and Loret, E (1999) Circular dichroism and molecular modeling of the E. coli TolA periplasmic domains. Biospectroscopy 5:189-98 |
|---|---|
| Abstract |
Colicins are killer proteins that use envelope proteins from the outer and the inner membranes to reach their cellular target in susceptible cells of Escherichia coli. Each group A colicin uses a combination of Tol proteins to cross the outer membrane of gram-negative bacteria and to exert their killing activity. The TolA protein, necessary for the import of all the group A colicins, is a 421-amino acid residue protein composed of three domains (TolAI, TolAII, and TolAIII). TolAIII interacts with the N-terminal domain of colicin A (AT1). Analytical ultracentrifugation reveals that TolAII and TolAIII are monomer structures, TolAII has an elongated structure, and TolAIII is rather globular. Circular dichroism (CD) spectra were done with TolAII-III, TolAII, TolAIII, AT1, and the AT1-TolAII-III complex. TolA CD spectra reveal the presence of alpha-helix structure in aqueous solution and the intensity of the a-helix signal is the highest with TolAII. Few structural changes are observed with the complex AT1-TolAII-III. Molecular modeling was done for TolAII-III, taking into account CD and ultracentrifugation data and show that domain II can adopt a barrel structure made of three twisted alpha-helices similar to coiled coil helices while domain III can adopt a globular structure. |
| Links |
PubMed Online version:<189::AID-BSPY8>3.0.CO;2-O 10.1002/(SICI)1520-6343(1999)5:3<189::AID-BSPY8>3.0.CO;2-O |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Centrifugation; Chromatography, High Pressure Liquid; Circular Dichroism; Colicins/chemistry; Colicins/metabolism; Escherichia coli/chemistry; Escherichia coli Proteins; Models, Molecular; Peptide Fragments/chemistry; Peptide Fragments/isolation & purification; Periplasm/chemistry; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification |
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