Abstract:
: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.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Mechaly AE,Bellomio A,Morante K,Agirre J,Gil-Cartón D,Valle M,González-Mañas JM,Guérin DMdoi
10.1016/j.jsb.2012.06.003subject
Has Abstractpub_date
2012-11-01 00:00:00pages
312-7issue
2eissn
1047-8477issn
1095-8657pii
S1047-8477(12)00183-9journal_volume
180pub_type
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