A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
| Autor: | Jeremy H. Lakey, F. G. van der Goot, Franc Pattus, Juan Manuel González-Mañas |
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| Rok vydání: | 1991 |
| Předmět: |
Multidisciplinary
Protein Conformation Chemistry Thermolysin Colicins Membrane Proteins Hydrogen-Ion Concentration Peptide Fragments Molten globule Kinetics Structure-Activity Relationship Crystallography Protein structure Membrane Cytoplasm Colicin Liposomes Protein folding Protein secondary structure |
| Zdroj: | Nature. 354:408-410 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/354408a0 |
| Popis: | THE 'molten' globular conformation of a protein is compact with a native secondary structure but a poorly defined tertiary structure1,2. Molten globular states are intermediates in protein folding and unfolding3–5 and they may be involved in the translocation or insertion of proteins into membranes6. Here we investigate the membrane insertion of the pore-forming domain of colicin A, a bacteriocin that depolarizes the cytoplasmic membrane of sensitive cells7–9. We find that this poreforming domain, the insertion of which depends on pH (refs 10,11), undergoes a native to molten globule transition at acidic pH. The variation of the kinetic constant of membrane insertion of the protein into negatively charged lipid vesicles as a function of the interfacial pH correlates with the appearance of the acidic molten globular state, indicating that this state could be an intermediate formed during the insertion of colicin A into membranes. |
| Databáze: | OpenAIRE |
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