title: Structure of bacteriocin AS-48: from soluble state to membrane bound state.
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.
authors: Grupo de Cristalografía Macromolecular y Biología Estructural, Instituto de Química Física Rocasolano, Consejo Superior de Investigaciones Científicas, Serrano 119, E-28006, Madrid, Spain.
authors: M J
authors: MJ
authors: Sánchez-Barrena
authors: M
authors: M
authors: Martínez-Ripoll
authors: A
authors: A
authors: Gálvez
authors: E
authors: E
authors: Valdivia
authors: M
authors: M
authors: Maqueda
authors: V
authors: V
authors: Cruz
authors: A
authors: A
authors: Albert
mesh_terms: D001426:Bacterial Proteins; D002462:Cell Membrane / Q000378:metabolism; D018360:Crystallography, X-Ray; D006094:Gram-Positive Bacteria / Q000737:chemistry* / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D014867:Water / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D010455:Peptides; D014867:Water; C051034:BacA protein, Enterococcus faecalis