Global structural rearrangement of the cell penetrating ribonuclease colicin E3 on interaction with phospholipid membranes.

Journal article

Nuclease type colicins and related bacteriocins possess the unprecedented ability to translocate an enzymatic polypeptide chain across the Gram-negative cell envelope. Here we use the rRNase domain of the cytotoxic ribonuclease colicin E3 to examine the structural changes on its interaction with the membrane. Using phospholipid vesicles as model membranes we show that anionic membranes destabilize the nuclease domain of the rRNase type colicin E3. Intrinsic tryptophan fluorescence and circula...

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Authors: Mosbahi, K; Walker, D; James, R; Moore, G; Kleanthous, K

• Journal: Protein science : a publication of the Protein Society
• Volume: 15
• Issue: 3
• Pages: 620-627
• Publication date: 2006-03-01
• DOI: 10.1110/ps.051890306
• EISSN: 1469-896X
• ISSN: 0961-8368
• Language: English
• Keywords: Protein Structure, Tertiary; Anions; Protein Binding; Ribonucleases; Protein Denaturation; Static Electricity; Osmolar Concentration; Colicins; Circular Dichroism; Phospholipids; Calorimetry; Protein Transport; Thermodynamics