Structure of bacteriocin AS-48: from soluble state to membrane bound state |
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Authors: | Sánchez-Barrena M J Martínez-Ripoll M Gálvez A Valdivia E Maqueda M Cruz V Albert A |
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Institution: | Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto de Química Física Rocasolano, Consejo Superior de Investigaciones Científicas, Serrano 119, E-28006, Madrid, Spain. |
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Abstract: | The bacteriocin AS-48 is a membrane-interacting peptide, which displays a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. The NMR structure of AS-48 at pH 3 has been solved. The analysis of this structure suggests that the mechanism of AS-48 anti-bacterial activity involves the accumulation of positively charged molecules at the membrane surface leading to a disruption of the membrane potential. Here, we report the high-resolution crystal structure of AS-48 and sedimentation equilibrium experiments showing that this bacteriocin is able to adopt different oligomeric structures according to the physicochemical environment. The analysis of these structures suggests a mechanism for molecular function of AS-48 involving a transition from a water-soluble form to a membrane-bound state upon membrane binding. |
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Keywords: | bacteriocin cyclic peptide cationic antibacterial peptides protein crystallography protein-membrane interaction |
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