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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Journal of structural biology

Pores of the toxin FraC assemble into 2D hexagonal clusters in both crystal structures and model membranes

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of structural biology - 21 Jun 2012

Mechaly AE, Bellomio A, Morante K, Agirre J, Gil-Cartón D, Valle M, González-Mañas JM, Guérin DM

Link to Pubmed [PMID] – 22728830

J. Struct. Biol. 2012 Nov;180(2):312-7

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.

https://www.ncbi.nlm.nih.gov/pubmed/22728830