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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.

Citation

M J Sánchez-Barrena, M Martínez-Ripoll, A Gálvez, E Valdivia, M Maqueda, V Cruz, A Albert. Structure of bacteriocin AS-48: from soluble state to membrane bound state. Journal of molecular biology. 2003 Nov 28;334(3):541-9

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PMID: 14623193

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