Download MendeleyStructure of Bacteriocin as-48: From Soluble State to Membrane Bound State
Sanchez-Barrena, M.J., Martinez-Ripoll, M., Galvez, A., Valdivia, E., Maqueda, M., Cruz, V., Albert, A.(2003) J Mol Biol 334: 541
- PubMed: 14623193
- DOI: https://doi.org/10.1016/j.jmb.2003.09.060
- Primary Citation of Related Structures:
1O82, 1O83, 1O84 - PubMed 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.
Organizational Affiliation:
Grupo de Cristalograf¨ªa Macromolecular y Biolog¨ªa Estructural, Instituto de Qu¨ªmica F¨ªsica Rocasolano, Consejo Superior de Investigaciones Cient¨ªficas, Serrano 119, E-28006, Madrid, Spain.
