INVESTIGADORES
BELLOMIO Augusto
artículos
Título:
Pores of the toxin FraC assemble into 2D hexagonal clusters in both crystal structures and model membranes
Autor/es:
MECHALY AE; BELLOMIO A; MORANTE K; AGIRRE J; GIL-CARTÓN D; VALLE M; GONZALEZ-MAÑAS JM; GUÉRIN DM
Revista:
JOURNAL OF STRUCTURAL BIOLOGY
Editorial:
ACADEMIC PRESS INC ELSEVIER SCIENCE
Referencias:
Lugar: Amsterdam; Año: 2012
ISSN:
1047-8477
Resumen:
The recent high-resolution structure of the toxin FraC derived from the
sea anemone Actinia fragacea has provided new insight into the mechanism
of pore formation by actinoporins. In this work, we report two new
crystal forms of FraC in its oligomeric prepore conformation. Together
with the previously reported structure, these two new structures reveal
that ring-like nonamers of the toxin assemble into compact
two-dimensional hexagonal arrays. This supramolecular organization is
maintained in different relative orientations adopted by the oligomers
within the crystal layers. Analyses of the aggregation of FraC pores in
both planar and curved (vesicles) model membranes show similar 2D
hexagonal arrangements. Our observations support a model in which
hexagonal pore-packing is a clustering mechanism that maximizes
toxin-driven membrane damage in the target cell.